MolNFT v1 · #127092 · protein
Tmb-1. structural insights into tmb-1 and the role of residue 119 and 228 in substrate and inhibitor binding
5MMD · Metallo-beta-lactamase 1: “Tmb-1. structural insights into tmb-1 and the role of residue 119 and 228 in substrate and inhibitor binding”. X-ray diffraction, 2 ligands (ZN, CL), 3 pockets (best druggability 0.82). MolNFT v1 #127092…
- PDB
- 5MMD
- Type
- protein
- Length
- 439 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallo-beta-lactamase 1
- UniProt
- T2HNV0
- Ligands
- ZN, CL
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Metallo-beta-lactamase 1 | protein | 221 | 27% helix, 31% strand | T2HNV0 |
| F | Metallo-beta-lactamase 1 | protein | 218 | 27% helix, 34% strand | T2HNV0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 726 | 0.82 | 0.86 | 71 | CL |
| 2 | 264 | 0.56 | 0.77 | 33 | empty |
| 3 | 139 | 0.48 | 0.78 | 25 | empty |
Interfaces
1 interface between chains.
- E–F · 811 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5MMD · TMB-1. Structural insights into TMB-1 and the role of residue 119 and 228 in substrate… · the same entry in another collection · chain E against E, 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 T2HNV0
- Elsewhere: RCSB PDB 5MMD · PDBe 5MMD · UniProt T2HNV0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.