MolNFT v1 · #13567 · protein
Crystal structure of pepv
1LFW: “Crystal structure of pepv”. X-ray diffraction, 2 ligands (AEP, ZN), 2 pockets (best druggability 0.65). MolNFT v1 #13567 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LFW
- Type
- protein
- Length
- 468 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pepv
- EC
- 3.4.13.3
- UniProt
- P45494
- Ligands
- AEP, ZN
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pepv (EC 3.4.13.3) | protein | 468 | 33% helix, 27% strand | P45494 |
Ligands and binding sites
- AEP · 3-[(1-amino-2-carboxy-ethyl)-hydroxy-phosphinoyl]-2-methyl-propionic acid · ligand · chains A
- ZN · Zinc ion · metal · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.65 | 0.82 | 46 | ZN, AEP |
| 2 | 176 | 0.50 | 0.77 | 37 | empty |
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 P45494
- Elsewhere: RCSB PDB 1LFW · PDBe 1LFW · UniProt P45494
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