MolNFT v1 · #144867 · protein
Crystal structure of a tailspike protein GP49 from acinetobacter baumannii bacteriophage FRI1, a capsular polysaccharide depolymerase
6C72 · Particle-associated glycoside hydrolase: “Crystal structure of a tailspike protein GP49 from acinetobacter baumannii bacteriophage FRI1, a capsular…”. X-ray diffraction, 1 ligand (ZN), 12 pockets (best druggability 0.84). MolNFT v1…
- PDB
- 6C72
- Type
- protein
- Length
- 1,737 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Particle-associated glycoside hydrolase
- UniProt
- A0A0H4TJ34
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Particle-associated glycoside hydrolase | protein | 579 | 7% helix, 43% strand | A0A0H4TJ34 |
Ligands and binding sites
- ZN · Zinc ion · metal · 40 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 902 | 0.84 | 0.86 | 121 | ZN |
| 2 | 232 | 0.82 | 0.94 | 36 | empty |
| 3 | 550 | 0.81 | 0.87 | 62 | ZN |
| 4 | 357 | 0.68 | 0.82 | 58 | empty |
| 5 | 462 | 0.64 | 0.77 | 30 | empty |
Interfaces
3 interfaces between chains.
- A–B · 3557 Ų buried · 57 hydrogen bonds · protein-protein
- A–C · 3551 Ų buried · 61 hydrogen bonds · protein-protein
- B–C · 3481 Ų buried · 60 hydrogen bonds · protein-protein
Compared structures
- 6C72 · Crystal structure of a tailspike protein gp49 from Acinetobacter baumannii bacteriophage… · 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 A0A0H4TJ34
- Elsewhere: RCSB PDB 6C72 · PDBe 6C72 · UniProt A0A0H4TJ34
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