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Crystal structure of the molybdenum cofactor biosynthesis protein moba (protein fa) from escherichia COLI at near atomic resolution

Analyse Crystal structure of the molybdenum cofactor biosynthesis protein moba (protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E5K
Type: protein
Length: 188 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Molybdopterin-guanine dinucleotide biosynthesis protein a
UniProt: P32173
Ligands: LI
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Molybdopterin-guanine dinucleotide biosynthesis protein a	protein	188	32% helix, 21% strand	P32173

Ligands and binding sites

LI · Lithium ion · metal · chains A
CIT · Citric acid · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	214	0.50	0.76	36	empty

Compared structures

1E5K · Crystal structure of the molybdenum cofactor biosynthesis protein moba (protein fa) from… · the same entry in another collection · chain A against A, TM-score 1.00
P32173 · AlphaFold monomer V2.0 prediction for molybdenum cofactor guanylyltransferase (P32173) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P32173
Elsewhere: RCSB PDB 1E5K · PDBe 1E5K · UniProt P32173

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