MolNFT v1 · #161594 · protein

Dimethyl disulfide inhibited sulfur oxygenase reductase

6QJC · Sulfur OXYGENASE/REDUCTASE: “Dimethyl disulfide inhibited sulfur oxygenase reductase”. X-ray diffraction, 1 ligand (FE), 12 pockets (best druggability 0.80). MolNFT v1 #161594 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6QJC
Type: protein
Length: 1,228 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulfur OXYGENASE/REDUCTASE
EC: 1.13.11.55
UniProt: P29082
Ligands: FE
Pockets: 12 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Sulfur OXYGENASE/REDUCTASE (EC 1.13.11.55)	protein	307	36% helix, 30% strand	P29082

Ligands and binding sites

FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	643	0.80	0.85	93	empty
2	624	0.80	0.85	85	empty
3	566	0.80	0.85	81	empty
4	648	0.80	0.84	92	empty
5	97	0.75	0.95	18	empty

Interfaces

6 interfaces between chains.

C–D · 1288 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1286 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 1283 Å² buried · 10 hydrogen bonds · protein-protein
B–D · 1274 Å² buried · 11 hydrogen bonds · protein-protein
A–D · 14 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (oxidation, nonstandard).

Compared structures

6QJC · Dimethyl disulfide inhibited sulfur oxygenase reductase · the same entry in another collection · chain A against A, TM-score 1.00
P29082 · AlphaFold monomer V2.0 prediction for sulfur OXYGENASE/REDUCTASE (P29082) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P29082
Elsewhere: RCSB PDB 6QJC · PDBe 6QJC · UniProt P29082

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