MolNFT v1 · #173193 · protein
L254N mutant of carboxypeptidase T from thermoactinomyces vulgaris N- sulfamoyl-L-valine
7ARU: “L254N mutant of carboxypeptidase T from thermoactinomyces vulgaris N- sulfamoyl-L-valine”. X-ray diffraction, 3 ligands (NO5, CA, ZN). MolNFT v1 #173193 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7ARU
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29068
- Ligands
- NO5, CA, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 323 | — | P29068 |
Ligands and binding sites
- NO5 · (2~{S})-3-methyl-2-(sulfamoylamino)butanoic acid · ligand · chains A
- CA · Calcium ion · metal · 5 copies · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7ARU · L254N mutant of carboxypeptidase T from Thermoactinomyces vulgaris N-sulfamoyl-L-valine · the same entry in another collection · chain A against A, TM-score 1.00
- P29068 · AlphaFold monomer V2.0 prediction for carboxypeptidase T (P29068) · 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 P29068
- Elsewhere: RCSB PDB 7ARU · PDBe 7ARU · UniProt P29068
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