Phosphorus in PDB 1ah4: Pig Aldose Reductase, Holo Form

All present enzymatic activity of Pig Aldose Reductase, Holo Form:
1.1.1.21;

The structure of Pig Aldose Reductase, Holo Form, PDB code: 1ah4 was solved by D.Moras, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.090, 68.090, 153.350, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 28.5

The binding sites of Phosphorus atom in the Pig Aldose Reductase, Holo Form (pdb code 1ah4). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the Pig Aldose Reductase, Holo Form, PDB code: 1ah4:
Jump to Phosphorus binding site number: 1; 2; 3;

Phosphorus binding site 1 out of 3 in the Pig Aldose Reductase, Holo Form


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Pig Aldose Reductase, Holo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:P318 b:41.1 occ:1.00 PA A:NAP318 0.0 41.1 1.0 O1A A:NAP318 1.5 39.0 1.0 O2A A:NAP318 1.5 32.9 1.0 O5B A:NAP318 1.6 35.3 1.0 O3 A:NAP318 1.6 40.6 1.0 C5B A:NAP318 2.7 33.4 1.0 PN A:NAP318 3.0 41.3 1.0 O5D A:NAP318 3.2 39.1 1.0 H A:SER214 3.3 15.0 1.0 H A:LEU212 3.4 15.0 1.0 H A:LYS262 3.4 15.0 1.0 O1N A:NAP318 3.7 44.3 1.0 OG A:SER214 3.7 60.2 1.0 C5D A:NAP318 3.8 26.8 1.0 C4B A:NAP318 3.9 36.5 1.0 N A:SER214 3.9 50.7 1.0 CA A:SER210 3.9 39.7 1.0 CA A:SER214 4.0 57.1 1.0 O2N A:NAP318 4.0 35.3 1.0 CD A:PRO211 4.2 41.9 1.0 CB A:LEU212 4.2 37.1 1.0 O4B A:NAP318 4.3 36.7 1.0 N A:LEU212 4.3 36.9 1.0 C A:SER210 4.3 43.3 1.0 CG A:LEU212 4.3 35.7 1.0 HG A:SER214 4.4 15.0 1.0 N A:LYS262 4.4 32.7 1.0 CB A:SER214 4.4 55.5 1.0 N A:PRO211 4.5 42.9 1.0 CD1 A:LEU212 4.5 34.1 1.0 CB A:LYS262 4.6 37.4 1.0 H A:GLY213 4.6 15.0 1.0 H A:SER210 4.7 15.0 1.0 CB A:SER210 4.7 37.4 1.0 CA A:LEU212 4.7 37.5 1.0 O A:LYS262 4.8 33.8 1.0 HZ2 A:LYS21 4.8 15.0 1.0 N A:SER210 4.8 40.8 1.0 OG A:SER210 4.8 40.2 1.0 N A:GLY213 4.8 47.1 1.0 C A:LEU212 4.9 42.7 1.0 O A:SER210 4.9 41.9 1.0

Phosphorus binding site 2 out of 3 in the Pig Aldose Reductase, Holo Form


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Pig Aldose Reductase, Holo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:P318 b:41.3 occ:1.00 PN A:NAP318 0.0 41.3 1.0 O2N A:NAP318 1.5 35.3 1.0 O1N A:NAP318 1.5 44.3 1.0 O3 A:NAP318 1.6 40.6 1.0 O5D A:NAP318 1.6 39.1 1.0 C5D A:NAP318 2.7 26.8 1.0 HZ2 A:LYS21 2.9 15.0 1.0 PA A:NAP318 3.0 41.1 1.0 OG A:SER214 3.2 60.2 1.0 HG A:SER214 3.2 15.0 1.0 O2A A:NAP318 3.4 32.9 1.0 HO3N A:NAP318 3.5 15.0 1.0 C3D A:NAP318 3.5 32.4 1.0 C4D A:NAP318 3.6 30.2 1.0 OG A:SER210 3.6 40.2 1.0 O1A A:NAP318 3.8 39.0 1.0 O5B A:NAP318 3.9 35.3 1.0 NZ A:LYS21 3.9 35.5 1.0 H A:SER210 3.9 15.0 1.0 O3D A:NAP318 4.0 40.8 1.0 C5B A:NAP318 4.1 33.4 1.0 O4D A:NAP318 4.1 34.7 1.0 CE3 A:TRP20 4.1 43.8 1.0 CB A:LYS262 4.1 37.4 1.0 CB A:SER214 4.1 55.5 1.0 CA A:SER210 4.1 39.7 1.0 C6N A:NAP318 4.2 26.4 1.0 HZ3 A:LYS21 4.3 15.0 1.0 HG A:SER210 4.4 15.0 1.0 CB A:SER210 4.4 37.4 1.0 N A:SER210 4.5 40.8 1.0 HZ1 A:LYS21 4.5 15.0 1.0 H A:LYS262 4.5 15.0 1.0 CE A:LYS21 4.6 43.1 1.0 CZ3 A:TRP20 4.6 45.8 1.0 CA A:SER214 4.7 57.1 1.0 C2D A:NAP318 4.8 27.8 1.0 CG A:LYS262 4.9 29.4 1.0 C1D A:NAP318 5.0 28.4 1.0 C5N A:NAP318 5.0 26.2 1.0

Phosphorus binding site 3 out of 3 in the Pig Aldose Reductase, Holo Form


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Pig Aldose Reductase, Holo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:P318 b:53.7 occ:1.00 P2B A:NAP318 0.0 53.7 1.0 O1X A:NAP318 1.5 46.9 1.0 O2X A:NAP318 1.5 47.9 1.0 O3X A:NAP318 1.5 52.3 1.0 O2B A:NAP318 1.6 49.5 1.0 HH21 A:ARG268 2.3 15.0 1.0 C2B A:NAP318 2.7 41.5 1.0 HZ1 A:LYS262 3.0 15.0 1.0 H A:VAL264 3.0 15.0 1.0 HO3A A:NAP318 3.2 20.0 1.0 HE A:ARG268 3.2 15.0 1.0 NH2 A:ARG268 3.3 58.1 1.0 HG A:SER263 3.5 15.0 1.0 O A:HOH586 3.5 55.5 0.7 OG A:SER263 3.5 31.7 1.0 C3B A:NAP318 3.5 37.7 1.0 HG1 A:THR265 3.6 15.0 1.0 OG1 A:THR265 3.7 35.0 1.0 H A:THR265 3.7 15.0 1.0 O3B A:NAP318 3.8 40.5 1.0 C1B A:NAP318 3.9 38.8 1.0 NZ A:LYS262 3.9 38.8 1.0 HH22 A:ARG268 3.9 15.0 1.0 NE A:ARG268 3.9 58.0 1.0 N A:VAL264 4.0 31.1 1.0 HZ2 A:LYS262 4.0 15.0 1.0 CA A:SER263 4.0 33.5 1.0 CZ A:ARG268 4.1 62.1 1.0 CG2 A:VAL264 4.3 37.4 1.0 CB A:SER263 4.3 31.2 1.0 N9A A:NAP318 4.4 34.7 1.0 N A:THR265 4.5 42.6 1.0 CB A:THR265 4.5 35.9 1.0 C A:SER263 4.6 31.3 1.0 HZ3 A:LYS262 4.6 15.0 1.0 O A:LYS262 4.6 33.8 1.0 C8A A:NAP318 4.6 33.9 1.0 CE A:LYS262 4.7 36.1 1.0 C4B A:NAP318 4.9 36.5 1.0 CD A:LYS262 5.0 37.9 1.0 O4B A:NAP318 5.0 36.7 1.0 CA A:VAL264 5.0 37.4 1.0

A.Urzhumtsev, F.Tete-Favier, A.Mitschler, J.Barbanton, P.Barth, L.Urzhumtseva, J.F.Biellmann, A.Podjarny, D.Moras. A 'Specificity' Pocket Inferred From the Crystal Structures of the Complexes of Aldose Reductase with the Pharmaceutically Important Inhibitors Tolrestat and Sorbinil. Structure V. 5 601 1997.
ISSN: ISSN 0969-2126
PubMed: 9195881
DOI: 10.1016/S0969-2126(97)00216-5