Research workbench

Silver-bound E. COLI malate dehydrogenase (C113 and C251)

Analyse Silver-bound E. COLI malate dehydrogenase (C113 and C251) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CGC
Type: protein
Length: 1,201 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P61889
Ligands: AG

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	—	protein	302	—	P61889
B	—	protein	301	—	P61889
D	—	protein	296	—	P61889

Ligands and binding sites

AG · Silver ion · metal · 16 copies · chains A, B, C, D

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

Compared structures

7CGC · Silver-bound E. coli Malate dehydrogenase (C113 and C251) · 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 B 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
Every structure of UniProt P61889
Elsewhere: RCSB PDB 7CGC · PDBe 7CGC · UniProt P61889

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