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The crystal structure of E.COLI malate dehydrogenase: a complex of the apoenzyme and citrate at 1.87 ångströms resolution

Analyse The crystal structure of E.COLI malate dehydrogenase: a complex of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CMD
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Malate dehydrogenase
EC: 1.1.1.37
UniProt: P61889
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Malate dehydrogenase (EC 1.1.1.37)	protein	312	49% helix, 17% strand	P61889

Ligands and binding sites

CIT · Citric acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	179	0.73	0.90	44	CIT

Compared structures

2CMD · The crystal structure of E.COLI malate dehydrogenase: a complex of the apoenzyme and… · the same entry in another collection · chain A against A, TM-score 1.00
P61889 · AlphaFold monomer V2.0 prediction for malate dehydrogenase (P61889) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P61889
Elsewhere: RCSB PDB 2CMD · PDBe 2CMD · UniProt P61889

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