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The active site of the molybdenum cofactor biosynthetic protein domain CNX1G

Analyse The active site of the molybdenum cofactor biosynthetic protein domain CNX1G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O8N
Type: protein
Length: 486 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Molybdopterin biosynthesis CNX1 protein
UniProt: Q39054
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Molybdopterin biosynthesis CNX1 protein	protein	162	49% helix, 21% strand	Q39054

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1081	0.82	0.83	142	empty

Interfaces

3 interfaces between chains.

A–B · 841 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 836 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 836 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1O8N · The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G · the same entry in another collection · chain A against A, TM-score 1.00
Q39054 · AlphaFold monomer V2.0 prediction for molybdopterin biosynthesis protein CNX1 (Q39054) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q39054
Elsewhere: RCSB PDB 1O8N · PDBe 1O8N · UniProt Q39054

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