MolNFT v1 · #81798 · protein
Carboxypeptidase T mutant L254N
3V38: “Carboxypeptidase T mutant L254N”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.54). MolNFT v1 #81798 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3V38
- 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
- ZN, SO4
- Pockets
- 2 · best druggability 0.54
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
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 25 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.54 | 0.85 | 22 | SO4, GOL |
| 2 | 54 | 0.28 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 3V38 · PDBe 3V38 · UniProt P29068
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