Phosphorus in PDB 1a8r: Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp

All present enzymatic activity of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp:
3.5.4.16;

The structure of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp, PDB code: 1a8r was solved by G.Auerbach, H.Nar, A.Bracher, A.Bacher, R.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	C 2 2 21 1
Cell size a, b, c (Å), α, β, γ (°)	314.950, 219.140, 131.410, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.6

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 45;

Binding sites:

The binding sites of Phosphorus atom in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp (pdb code 1a8r). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 45 binding sites of Phosphorus where determined in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp, PDB code: 1a8r:
Jump to Phosphorus binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Phosphorus binding site 1 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:P401 b:29.4 occ:1.00 PG A:GTP401 0.0 29.4 1.0 O1G A:GTP401 1.5 29.2 1.0 O2G A:GTP401 1.5 26.9 1.0 O3G A:GTP401 1.6 29.0 1.0 O3B A:GTP401 1.6 36.6 1.0 PB A:GTP401 2.9 30.6 1.0 NH1 B:ARG139 3.1 37.8 1.0 O1B A:GTP401 3.3 23.2 1.0 OG B:SER135 3.4 37.8 1.0 O2B A:GTP401 3.4 26.7 1.0 NH2 A:ARG185 3.5 44.6 1.0 NZ B:LYS136 3.7 27.7 1.0 NH1 A:ARG185 3.8 38.2 1.0 O A:HOH450 3.9 25.7 1.0 CZ A:ARG185 4.1 37.1 1.0 O3A A:GTP401 4.1 26.7 1.0 O A:HOH453 4.2 38.4 1.0 O A:HOH422 4.3 50.3 1.0 CB B:SER135 4.3 33.4 1.0 CZ B:ARG139 4.4 30.1 1.0 C3' A:GTP401 4.4 25.2 1.0 O3' A:GTP401 4.5 18.9 1.0 CE B:LYS136 4.6 29.4 1.0 O1A A:GTP401 4.6 20.9 1.0 O5' A:GTP401 4.7 35.6 1.0 CD B:ARG139 4.7 26.6 1.0 PA A:GTP401 4.8 29.4 1.0 NE B:ARG139 5.0 33.7 1.0 CE1 A:HIS113 5.0 27.9 1.0

Phosphorus binding site 2 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:P401 b:30.6 occ:1.00 PB A:GTP401 0.0 30.6 1.0 O1B A:GTP401 1.4 23.2 1.0 O2B A:GTP401 1.4 26.7 1.0 O3A A:GTP401 1.6 26.7 1.0 O3B A:GTP401 1.6 36.6 1.0 PA A:GTP401 2.9 29.4 1.0 PG A:GTP401 2.9 29.4 1.0 O1A A:GTP401 3.1 20.9 1.0 O1G A:GTP401 3.1 29.2 1.0 O5' A:GTP401 3.6 35.6 1.0 NH2 A:ARG185 3.7 44.6 1.0 O3G A:GTP401 3.7 29.0 1.0 NE2 A:HIS113 3.9 19.7 1.0 O A:HOH443 4.0 52.0 1.0 O2G A:GTP401 4.0 26.9 1.0 CE1 A:HIS113 4.0 27.9 1.0 O2A A:GTP401 4.1 33.2 1.0 C5' A:GTP401 4.2 30.1 1.0 O A:HOH422 4.3 50.3 1.0 NZ B:LYS136 4.4 27.7 1.0 CZ A:ARG185 4.6 37.1 1.0 C3' A:GTP401 4.9 25.2 1.0 O A:HOH454 4.9 33.2 1.0 NH1 A:ARG185 5.0 38.2 1.0

Phosphorus binding site 3 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:P401 b:29.4 occ:1.00 PA A:GTP401 0.0 29.4 1.0 O2A A:GTP401 1.5 33.2 1.0 O1A A:GTP401 1.5 20.9 1.0 O5' A:GTP401 1.6 35.6 1.0 O3A A:GTP401 1.7 26.7 1.0 C5' A:GTP401 2.7 30.1 1.0 PB A:GTP401 2.9 30.6 1.0 O3B A:GTP401 3.2 36.6 1.0 O1B A:GTP401 3.3 23.2 1.0 CG2 B:THR87 3.6 41.6 1.0 C4' A:GTP401 3.9 26.0 1.0 OG1 B:THR87 3.9 53.7 1.0 O2B A:GTP401 4.0 26.7 1.0 NZ B:LYS136 4.2 27.7 1.0 CB B:THR87 4.3 40.0 1.0 C3' A:GTP401 4.3 25.2 1.0 CE B:LYS136 4.4 29.4 1.0 O A:HOH443 4.4 52.0 1.0 PG A:GTP401 4.8 29.4 1.0 O3' A:GTP401 4.8 18.9 1.0

Phosphorus binding site 4 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 4 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:P402 b:26.9 occ:1.00 PG B:GTP402 0.0 26.9 1.0 O2G B:GTP402 1.5 38.7 1.0 O1G B:GTP402 1.5 23.4 1.0 O3G B:GTP402 1.6 26.8 1.0 O3B B:GTP402 1.6 31.4 1.0 PB B:GTP402 2.9 31.6 1.0 NH1 C:ARG139 3.0 41.0 1.0 O2B B:GTP402 3.3 31.7 1.0 O1B B:GTP402 3.4 31.5 1.0 OG C:SER135 3.5 23.9 1.0 NH2 B:ARG185 3.6 29.4 1.0 NZ C:LYS136 3.7 23.0 1.0 O B:HOH553 3.8 27.8 1.0 NH1 B:ARG185 3.8 22.8 1.0 O B:HOH556 4.0 31.2 1.0 O3A B:GTP402 4.1 33.7 1.0 O B:HOH515 4.1 55.6 1.0 CZ C:ARG139 4.1 34.4 1.0 CZ B:ARG185 4.2 25.1 1.0 CB C:SER135 4.5 21.5 1.0 C3' B:GTP402 4.5 24.7 1.0 CD C:ARG139 4.6 26.5 1.0 CE C:LYS136 4.6 25.8 1.0 O1A B:GTP402 4.7 30.1 1.0 O3' B:GTP402 4.7 18.8 1.0 NE C:ARG139 4.7 39.7 1.0 O5' B:GTP402 4.8 22.7 1.0 PA B:GTP402 4.9 28.5 1.0 CA B:GLY186 4.9 27.4 1.0 CE1 B:HIS113 4.9 26.1 1.0

Phosphorus binding site 5 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 5 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:P402 b:31.6 occ:1.00 PB B:GTP402 0.0 31.6 1.0 O1B B:GTP402 1.4 31.5 1.0 O2B B:GTP402 1.4 31.7 1.0 O3B B:GTP402 1.6 31.4 1.0 O3A B:GTP402 1.6 33.7 1.0 PG B:GTP402 2.9 26.9 1.0 PA B:GTP402 2.9 28.5 1.0 O1G B:GTP402 3.1 23.4 1.0 O1A B:GTP402 3.2 30.1 1.0 O5' B:GTP402 3.6 22.7 1.0 NH2 B:ARG185 3.7 29.4 1.0 O3G B:GTP402 3.7 26.8 1.0 NE2 B:HIS113 3.8 27.6 1.0 O2G B:GTP402 3.9 38.7 1.0 CE1 B:HIS113 4.0 26.1 1.0 O B:HOH545 4.1 63.5 1.0 O2A B:GTP402 4.1 36.5 1.0 C5' B:GTP402 4.1 27.3 1.0 O B:HOH515 4.2 55.6 1.0 NZ C:LYS136 4.2 23.0 1.0 CZ B:ARG185 4.6 25.1 1.0 O B:HOH557 4.8 28.0 1.0 NH1 B:ARG185 4.8 22.8 1.0 C3' B:GTP402 5.0 24.7 1.0

Phosphorus binding site 6 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 6 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:P402 b:28.5 occ:1.00 PA B:GTP402 0.0 28.5 1.0 O2A B:GTP402 1.4 36.5 1.0 O1A B:GTP402 1.5 30.1 1.0 O5' B:GTP402 1.6 22.7 1.0 O3A B:GTP402 1.7 33.7 1.0 C5' B:GTP402 2.7 27.3 1.0 PB B:GTP402 2.9 31.6 1.0 O3B B:GTP402 3.3 31.4 1.0 O1B B:GTP402 3.3 31.5 1.0 CG2 C:THR87 3.7 25.1 1.0 C4' B:GTP402 3.8 22.9 1.0 NZ C:LYS136 4.0 23.0 1.0 O2B B:GTP402 4.1 31.7 1.0 OG1 C:THR87 4.1 41.8 1.0 CE C:LYS136 4.3 25.8 1.0 O B:HOH545 4.4 63.5 1.0 C3' B:GTP402 4.4 24.7 1.0 CB C:THR87 4.5 37.9 1.0 PG B:GTP402 4.9 26.9 1.0 O3' B:GTP402 4.9 18.8 1.0

Phosphorus binding site 7 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 7 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ C:P403 b:25.5 occ:1.00 PG C:GTP403 0.0 25.5 1.0 O1G C:GTP403 1.5 28.6 1.0 O2G C:GTP403 1.5 24.1 1.0 O3G C:GTP403 1.6 31.6 1.0 O3B C:GTP403 1.7 27.5 1.0 PB C:GTP403 3.0 28.7 1.0 NH1 D:ARG139 3.1 26.4 1.0 O1B C:GTP403 3.4 34.1 1.0 OG D:SER135 3.5 35.1 1.0 O2B C:GTP403 3.5 32.4 1.0 NH1 C:ARG185 3.6 38.5 1.0 O C:HOH573 3.7 30.0 1.0 NH2 C:ARG185 3.8 43.3 1.0 NZ D:LYS136 3.9 19.9 1.0 O C:HOH576 3.9 28.4 1.0 CZ C:ARG185 4.1 37.5 1.0 O3A C:GTP403 4.2 26.2 1.0 O C:HOH545 4.2 52.8 1.0 CB D:SER135 4.3 26.1 1.0 CZ D:ARG139 4.4 25.4 1.0 C3' C:GTP403 4.5 27.1 1.0 O1A C:GTP403 4.6 30.9 1.0 CE D:LYS136 4.6 17.4 1.0 O3' C:GTP403 4.7 20.4 1.0 CD D:ARG139 4.7 19.4 1.0 O5' C:GTP403 4.8 31.7 1.0 CE1 C:HIS113 4.9 26.7 1.0 PA C:GTP403 4.9 29.6 1.0 CA C:GLY186 4.9 25.1 1.0

Phosphorus binding site 8 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 8 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ C:P403 b:28.7 occ:1.00 PB C:GTP403 0.0 28.7 1.0 O2B C:GTP403 1.4 32.4 1.0 O1B C:GTP403 1.5 34.1 1.0 O3A C:GTP403 1.6 26.2 1.0 O3B C:GTP403 1.6 27.5 1.0 PA C:GTP403 2.9 29.6 1.0 PG C:GTP403 3.0 25.5 1.0 O1A C:GTP403 3.1 30.9 1.0 O1G C:GTP403 3.2 28.6 1.0 O5' C:GTP403 3.6 31.7 1.0 NH2 C:ARG185 3.7 43.3 1.0 O3G C:GTP403 3.8 31.6 1.0 NE2 C:HIS113 3.9 24.2 1.0 CE1 C:HIS113 4.0 26.7 1.0 O C:HOH566 4.1 51.5 1.0 O2A C:GTP403 4.1 27.5 1.0 O2G C:GTP403 4.1 24.1 1.0 O C:HOH545 4.1 52.8 1.0 C5' C:GTP403 4.2 32.6 1.0 NZ D:LYS136 4.4 19.9 1.0 CZ C:ARG185 4.5 37.5 1.0 NH1 C:ARG185 4.8 38.5 1.0 O C:HOH577 4.9 38.2 1.0 C3' C:GTP403 4.9 27.1 1.0

Phosphorus binding site 9 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 9 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ C:P403 b:29.6 occ:1.00 PA C:GTP403 0.0 29.6 1.0 O2A C:GTP403 1.5 27.5 1.0 O1A C:GTP403 1.5 30.9 1.0 O5' C:GTP403 1.6 31.7 1.0 O3A C:GTP403 1.7 26.2 1.0 C5' C:GTP403 2.7 32.6 1.0 PB C:GTP403 2.9 28.7 1.0 O3B C:GTP403 3.3 27.5 1.0 O1B C:GTP403 3.3 34.1 1.0 CG2 D:THR87 3.7 35.4 1.0 C4' C:GTP403 3.8 26.0 1.0 O2B C:GTP403 4.0 32.4 1.0 NZ D:LYS136 4.2 19.9 1.0 OG1 D:THR87 4.3 50.1 1.0 O C:HOH566 4.3 51.5 1.0 C3' C:GTP403 4.3 27.1 1.0 CE D:LYS136 4.4 17.4 1.0 CB D:THR87 4.5 33.6 1.0 O3' C:GTP403 4.8 20.4 1.0 PG C:GTP403 4.9 25.5 1.0

Phosphorus binding site 10 out of 45 in the Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 10 of Gtp Cyclohydrolase I (H112S Mutant) in Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ D:P404 b:28.4 occ:1.00 PG D:GTP404 0.0 28.4 1.0 O1G D:GTP404 1.5 28.6 1.0 O2G D:GTP404 1.5 35.6 1.0 O3G D:GTP404 1.6 33.2 1.0 O3B D:GTP404 1.7 41.8 1.0 PB D:GTP404 2.9 36.1 1.0 NH1 E:ARG139 3.1 39.8 1.0 O1B D:GTP404 3.3 31.7 1.0 O2B D:GTP404 3.4 33.0 1.0 NH2 D:ARG185 3.4 43.9 1.0 OG E:SER135 3.5 36.5 1.0 NH1 D:ARG185 3.7 34.7 1.0 NZ E:LYS136 3.7 28.3 1.0 O D:HOH572 3.8 26.5 1.0 O D:HOH544 3.9 65.0 1.0 CZ D:ARG185 4.0 33.8 1.0 O3A D:GTP404 4.1 32.4 1.0 O D:HOH575 4.2 35.5 1.0 CZ E:ARG139 4.3 33.3 1.0 CB E:SER135 4.4 30.7 1.0 C3' D:GTP404 4.5 31.1 1.0 CE E:LYS136 4.5 28.1 1.0 O1A D:GTP404 4.6 31.6 1.0 O3' D:GTP404 4.7 28.2 1.0 O5' D:GTP404 4.7 33.2 1.0 CD E:ARG139 4.7 29.6 1.0 PA D:GTP404 4.9 32.9 1.0 NE E:ARG139 4.9 37.8 1.0 CE1 D:HIS113 4.9 25.3 1.0 CA D:GLY186 5.0 37.2 1.0

J.Rebelo, G.Auerbach, G.Bader, A.Bracher, H.Nar, C.Hosl, N.Schramek, J.Kaiser, A.Bacher, R.Huber, M.Fischer. Biosynthesis of Pteridines. Reaction Mechanism of Gtp Cyclohydrolase I. J.Mol.Biol. V. 326 503 2003.
ISSN: ISSN 0022-2836
PubMed: 12559918
DOI: 10.1016/S0022-2836(02)01303-7