Research workbench
Ethylene forming enzyme (efe) in complex with FE(II), L-arginine, and 2OG
Analyse Ethylene forming enzyme (efe) in complex with FE(II), L-arginine, and 2OG in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VP4
- Type
- protein
- Length
- 1,347 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 | 334 | — | P32021 |
| B | — | protein | 341 | — | P32021 |
| C | — | protein | 340 | — | 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
- 6VP4 · Ethylene forming enzyme (EFE) 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 6VP4 · PDBe 6VP4 · UniProt P32021
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