MolNFT v1 · #93011 · protein
Crystal structure of a putative cell adhesion protein (BACEGG_00536) from bacteroides eggerthii dsm 20697 at 1.67 a resolution
4GPV: “Crystal structure of a putative cell adhesion protein (BACEGG_00536) from bacteroides eggerthii dsm 20697 at…”. X-ray diffraction, 4 pockets (best druggability 0.59). MolNFT v1 #93011 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4GPV
- Type
- protein
- Length
- 655 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cell adhesion protein
- UniProt
- B7ADR8
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cell adhesion protein | protein | 327 | 4% helix, 48% strand | B7ADR8 |
| B | Putative cell adhesion protein | protein | 328 | 4% helix, 46% strand | B7ADR8 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 425 | 0.59 | 0.75 | 47 | TRS |
| 2 | 183 | 0.47 | 0.76 | 27 | empty |
| 3 | 70 | 0.32 | 0.75 | 20 | empty |
| 4 | 63 | 0.29 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 272 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4GPV · Crystal structure of a putative cell adhesion protein (BACEGG_00536) from Bacteroides… · 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 B7ADR8
- Elsewhere: RCSB PDB 4GPV · PDBe 4GPV · UniProt B7ADR8
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