MolNFT v1 · #163564 · protein

Structure of azospirillum brasilense glutamate synthase in A6B4 oligomeric state.

6S6U: “Structure of azospirillum brasilense glutamate synthase in A6B4 oligomeric state.”. Electron microscopy, 4 ligands (SF4, FMN, F3S). MolNFT v1 #163564 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6S6U
Type: protein
Length: 10,720 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q05755, Q05756
Ligands: SF4, FMN, F3S, FAD

Structure

electron microscopy · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	—	protein	1472	—	Q05755
G, H, I, J	—	protein	472	—	Q05756

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · 8 copies · chains G, H, I, J
FMN · Flavin mononucleotide · ligand · 6 copies · chains A, B, C, D, E, F
F3S · FE3-S4 cluster · ligand · 6 copies · chains A, B, C, D, E, F
FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains G, H, I, J

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

Compared structures

6S6U · Structure of Azospirillum brasilense Glutamate Synthase in a6b4 oligomeric state. · the same entry in another collection · chain J against J, TM-score 1.00
Q05755 · AlphaFold monomer V2.0 prediction for glutamate synthase [NADPH] large chain (Q05755) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 Q05755
Every structure of UniProt Q05756
Elsewhere: RCSB PDB 6S6U · PDBe 6S6U · UniProt Q05755 · UniProt Q05756

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