MolNFT v1 · #137375 · protein
Structure of the R105A mutant catalytic trimer of escherichia COLI aspartate transcarbamoylase at 2.0-a resolution
5VMQ: “Structure of the R105A mutant catalytic trimer of escherichia COLI aspartate transcarbamoylase at 2.0-a…”. X-ray diffraction, 2 ligands (CA, CL). MolNFT v1 #137375 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VMQ
- Type
- protein
- Length
- 896 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B7MLQ3
- Ligands
- CA, CL
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 298 | — | B7MLQ3 |
| B | — | protein | 289 | — | B7MLQ3 |
| C | — | protein | 309 | — | B7MLQ3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VMQ · Structure of the R105A mutant catalytic trimer of escherichia COLI aspartate… · the same entry in another collection · chain A against A, TM-score 1.00
- B7MLQ3 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase (B7MLQ3) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 B7MLQ3
- Elsewhere: RCSB PDB 5VMQ · PDBe 5VMQ · UniProt B7MLQ3
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