Research workbench
G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from thermoactinomyces vulgaris with N-sulfamoyl-L-phenylalanine
Analyse G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IAV
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase T
- EC
- 3.4.17.18
- UniProt
- P29068
- Ligands
- CXA, CA, ZN, SO4
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase T (EC 3.4.17.18) | protein | 323 | 36% helix, 17% strand | P29068 |
Ligands and binding sites
- CXA · Phenylalanine-N-sulfonamide · ligand · chains A
- CA · Calcium ion · metal · 5 copies · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.61 | 0.86 | 27 | CXA, SO4 |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4IAV · G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces… · 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 4IAV · PDBe 4IAV · UniProt P29068
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