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MolNFT v2 · #190305 · protein

TmHydABC- T. maritima bifurcating hydrogenase with bridge domain closed

7P91: “TmHydABC- T. maritima bifurcating hydrogenase with bridge domain closed”. Electron microscopy at 2.8, 4 ligands (SF4, FES, FMN). MolNFT v2 #190305 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7P91
Type
protein
Length
2,681 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.8
Source
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 /…
UniProt
G4FFG1, G4FFG0, Q9S5X7
Ligands
SF4, FES, FMN, ZN

Structure

electron microscopy · resolution 2.8 · 5 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
a—protein642—G4FFG1
b—protein560—G4FFG0
c, C—protein156—Q9S5X7
A—protein554—G4FFG1
B—protein613—G4FFG0

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · 12 copies · chains a, A, b, B
  • FES · Fe2/s2 (inorganic) cluster · ligand · 7 copies · chains a, b, c, A, B, C
  • FMN · Flavin mononucleotide · ligand · 2 copies · chains b, B
  • ZN · Zinc ion · metal · 2 copies · chains b, B

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

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