MolNFT v1 · #8803 · protein
Methyl-coenzyme M reductase mcr-RED1-silent
1HBO: “Methyl-coenzyme M reductase mcr-RED1-silent”. X-ray diffraction. MolNFT v1 #8803 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1HBO
- Type
- protein
- Length
- 2,476 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11558, P11560, P11562
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 549 | — | P11558 |
| B, E | — | protein | 442 | — | P11560 |
| C, F | — | protein | 247 | — | P11562 |
Compared structures
- 1HBO · Methyl-coenzyme M reductase mcr-RED1-silent · the same entry in another collection · chain F against F, TM-score 1.00
- P11558 · AlphaFold monomer V2.0 prediction for methyl-coenzyme M reductase I subunit alpha (P11558) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P11560 · AlphaFold monomer V2.0 prediction for methyl-coenzyme M reductase I subunit beta (P11560) · a predicted model of the same protein · chain B against A, TM-score 1.00
- P11562 · AlphaFold monomer V2.0 prediction for methyl-coenzyme M reductase I subunit gamma (P11562) · 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 P11558
- Every structure of UniProt P11560
- Every structure of UniProt P11562
- Elsewhere: RCSB PDB 1HBO · PDBe 1HBO · UniProt P11558 · UniProt P11560 · UniProt P11562
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