MolNFT v1 · #37543 · protein

Anomalous substructure of moga

2G4R · Molybdopterin biosynthesis mog protein: “Anomalous substructure of moga”. X-ray diffraction, 1 ligand (CL), 5 pockets (best druggability 0.79). MolNFT v1 #37543 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2G4R
Type: protein
Length: 447 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Molybdopterin biosynthesis mog protein
Ligands: CL
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Molybdopterin biosynthesis mog protein	protein	153	46% helix, 17% strand	—
B	Molybdopterin biosynthesis mog protein	protein	151	47% helix, 18% strand	—
C	Molybdopterin biosynthesis mog protein	protein	143	43% helix, 18% strand	—

Ligands and binding sites

CL · Chloride ion · ion · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1088	0.79	0.81	123	empty
2	171	0.48	0.77	40	empty
3	91	0.45	0.80	20	empty
4	107	0.44	0.78	27	CL
5	76	0.32	0.75	17	empty

Interfaces

3 interfaces between chains.

A–C · 375 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 350 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 307 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2G4R · anomalous substructure of MogA · the same entry in another collection · 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
Elsewhere: RCSB PDB 2G4R · PDBe 2G4R

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