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MOEA E188Q

Analyse MOEA E188Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NQU
Type: protein
Length: 807 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Molybdopterin biosynthesis protein moea
UniProt: P12281
Pockets: 10 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Molybdopterin biosynthesis protein moea	protein	403	20% helix, 32% strand	P12281
B	Molybdopterin biosynthesis protein moea	protein	404	22% helix, 31% strand	P12281

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	586	0.76	0.83	70	empty
2	1080	0.76	0.78	84	GOL
3	634	0.67	0.76	61	GOL
4	314	0.63	0.80	34	GOL
5	107	0.54	0.83	16	empty

Interfaces

1 interface between chains.

A–B · 2322 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

2NQU · MoeA E188Q · the same entry in another collection · chain A against A, TM-score 1.00
P12281 · AlphaFold monomer V2.0 prediction for molybdopterin molybdenumtransferase (P12281) · a predicted model of the same protein · chain B 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 P12281
Elsewhere: RCSB PDB 2NQU · PDBe 2NQU · UniProt P12281

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