MolNFT v1 · #17199 · protein
Roles of HIS291-alpha and HIS146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase
1OLS: “Roles of HIS291-alpha and HIS146-beta' in the reductive acylation reaction catalyzed by human branched-chain…”. X-ray diffraction. MolNFT v1 #17199 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OLS
- Type
- protein
- Length
- 722 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12694, P21953
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 386 | — | P12694 |
| B | — | protein | 336 | — | P21953 |
Compared structures
- 1OLS · Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by… · the same entry in another collection · chain A against A, TM-score 1.00
- P21953 · AlphaFold monomer V2.0 prediction for 2-oxoisovalerate dehydrogenase subunit beta… · a predicted model of the same protein · chain B against A, TM-score 1.00
- P12694 · AlphaFold monomer V2.0 prediction for 2-oxoisovalerate dehydrogenase subunit alpha… · a predicted model of the same protein · 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 P12694
- Every structure of UniProt P21953
- Elsewhere: RCSB PDB 1OLS · PDBe 1OLS · UniProt P12694 · UniProt P21953
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