MolNFT v1 · #97131 · protein
Crystal structure of a putative cell adhesion protein (BACUNI_00621) from bacteroides uniformis atcc 8492 at 1.67 a resolution
4K4K: “Crystal structure of a putative cell adhesion protein (BACUNI_00621) from bacteroides uniformis atcc 8492 at…”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.72). MolNFT v1 #97131 on GenesisL1: 3D structure…
- PDB
- 4K4K
- Type
- protein
- Length
- 513 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cell adhesion protein
- UniProt
- A7UZ95
- Ligands
- CL
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cell adhesion protein | protein | 256 | 5% helix, 47% strand | A7UZ95 |
| B | Putative cell adhesion protein | protein | 257 | 7% helix, 47% strand | A7UZ95 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.72 | 0.79 | 74 | empty |
| 2 | 172 | 0.45 | 0.75 | 24 | empty |
| 3 | 89 | 0.34 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 640 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4K4K · Crystal structure of a putative cell adhesion protein (BACUNI_00621) from Bacteroides… · the same entry in another collection · chain A against A, TM-score 1.00
- A7UZ95 · AlphaFold monomer V2.0 prediction for putative fimbrium subunit FIM1C (A7UZ95) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 A7UZ95
- Elsewhere: RCSB PDB 4K4K · PDBe 4K4K · UniProt A7UZ95
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