Research workbench
Allophanate hydrolase complex from mycobacterium smegmatis, MSMEG0435- MSMEG0436
Analyse Allophanate hydrolase complex from mycobacterium smegmatis, MSMEG0435- MSMEG0436 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MML
- Type
- protein
- Length
- 1,997 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0QPL0, A0QPL1
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 289 | — | A0QPL0 |
| B, F | — | protein | 210 | — | A0QPL1 |
| C | — | protein | 290 | — | A0QPL0 |
| D, H | — | protein | 209 | — | A0QPL1 |
| E | — | protein | 292 | — | A0QPL0 |
| G | — | protein | 288 | — | A0QPL0 |
Compared structures
- 3MML · Allophanate Hydrolase Complex from Mycobacterium smegmatis, Msmeg0435-Msmeg0436 · the same entry in another collection · chain H against H, 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 A0QPL0
- Every structure of UniProt A0QPL1
- Elsewhere: RCSB PDB 3MML · PDBe 3MML · UniProt A0QPL0 · UniProt A0QPL1
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