MolNFT v1 · #148701 · protein

A. vinelandii vanadium nitrogenase, turnover state

6FEA: “A. vinelandii vanadium nitrogenase, turnover state”. X-ray diffraction, 7 ligands (HCA, D6N, CLF). MolNFT v1 #148701 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6FEA
Type: protein
Length: 2,074 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: C1DI25, C1DI23, C1DI24
Ligands: HCA, D6N, CLF, MG, ZN, CO3, H2S

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	—	protein	461	—	C1DI25
B, E	—	protein	464	—	C1DI23
C	—	protein	113	—	C1DI24
F	—	protein	111	—	C1DI24

Ligands and binding sites

HCA · 3-hydroxy-3-carboxy-adipic acid · ligand · 2 copies · chains A, B, D, E
D6N · FeV · ligand · 2 copies · chains A, D
CLF · FE(8)-S(7) cluster · ligand · 2 copies · chains A, B, D, E
MG · Magnesium ion · metal · 4 copies · chains B, E, C, F
ZN · Zinc ion · metal · 2 copies · chains A, E, B, D
CO3 · Carbonate ion · ion · 2 copies · chains A, D
H2S · Hydrosulfuric acid · ion · 2 copies · chains A, D

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

Compared structures

6FEA · A. vinelandii vanadium nitrogenase, turnover state · the same entry in another collection · chain A 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 C1DI25
Every structure of UniProt C1DI23
Every structure of UniProt C1DI24
Elsewhere: RCSB PDB 6FEA · PDBe 6FEA · UniProt C1DI25 · UniProt C1DI23 · UniProt C1DI24

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