MolNFT v1 · #113346 · protein
W228Y-investigation of the impact from residues W228 and Y233 in the metallo-beta-lactamase gim-1
5ACR · Gim-1 protein: “W228Y-investigation of the impact from residues W228 and Y233 in the metallo-beta-lactamase gim-1”. X-ray diffraction, 2 ligands (ZN, CA), 2 pockets (best druggability 0.36). MolNFT v1 #113346 on GenesisL1: 3D…
- PDB
- 5ACR
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gim-1 protein
- UniProt
- Q704V1
- Ligands
- ZN, CA
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Gim-1 protein | protein | 217 | 27% helix, 31% strand | Q704V1 |
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 | 88 | 0.36 | 0.75 | 18 | empty |
| 2 | 64 | 0.35 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 700 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
- 5ACR · W228Y-Investigation of the impact from residues W228 and Y233 in the… · the same entry in another collection · 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 Q704V1
- Elsewhere: RCSB PDB 5ACR · PDBe 5ACR · UniProt Q704V1
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