MolNFT v1 · #189226 · protein
Crystal structure of bacterial peptidase
7V6T · Murein dd-endopeptidase MEPS/MUREIN ld-carboxypeptidase: “Crystal structure of bacterial peptidase”. X-ray diffraction, 2 pockets (best druggability 0.34). MolNFT v1 #189226 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7V6T
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Murein dd-endopeptidase MEPS/MUREIN ld-carboxypeptidase
- EC
- 3.4.17.13
- UniProt
- P0AFV4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Murein dd-endopeptidase MEPS/MUREIN ld-carboxypeptidase (EC 3.4.17.13) | protein | 130 | 29% helix, 30% strand | P0AFV4 |
| B | Murein dd-endopeptidase MEPS/MUREIN ld-carboxypeptidase (EC 3.4.17.13) | protein | 120 | 32% helix, 31% strand | P0AFV4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.34 | 0.74 | 25 | empty |
| 2 | 81 | 0.33 | 0.75 | 25 | CIT, EDO |
Interfaces
1 interface between chains.
- A–B · 836 Ų buried · 13 hydrogen bonds · protein-protein
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 P0AFV4
- Elsewhere: RCSB PDB 7V6T · PDBe 7V6T · UniProt P0AFV4
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