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Ethylene forming enzyme (efe) D191E variant in complex with FE(II), L- arginine, and 2OG

Analyse Ethylene forming enzyme (efe) D191E variant in complex with FE(II), L… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VP5
Type: protein
Length: 1,349 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P32021
Ligands: AKG, FE

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	336	—	P32021
B	—	protein	343	—	P32021
C	—	protein	338	—	P32021
D	—	protein	332	—	P32021

Ligands and binding sites

AKG · 2-oxoglutaric acid · ligand · 4 copies · chains A, B, C, D
FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A, D

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

Compared structures

6VP5 · Ethylene forming enzyme (EFE) D191E variant in complex with Fe(II), L-arginine, and 2OG · the same entry in another collection · chain B against B, TM-score 1.00
P32021 · AlphaFold monomer V2.0 prediction for 2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming… · a predicted model of the same protein · chain C 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 P32021
Elsewhere: RCSB PDB 6VP5 · PDBe 6VP5 · UniProt P32021

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