Research workbench
Crystal structure of a COG1816 amidohydrolase (target efi-505188) from burkhoderia ambifaria, with bound zn
Analyse Crystal structure of a COG1816 amidohydrolase (target efi-505188) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GXW
- Type
- protein
- Length
- 733 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine deaminase
- EC
- 3.5.4.4
- UniProt
- Q0B6Q2
- Ligands
- ZN, CL
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine deaminase (EC 3.5.4.4) | protein | 369 | 57% helix, 13% strand | Q0B6Q2 |
| B | Adenosine deaminase (EC 3.5.4.4) | protein | 364 | 56% helix, 13% strand | Q0B6Q2 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 560 | 0.71 | 0.79 | 70 | empty |
| 2 | 96 | 0.61 | 0.88 | 22 | CL |
Interfaces
1 interface between chains.
- A–B · 280 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4GXW · Crystal structure of a cog1816 amidohydrolase (target EFI-505188) from Burkhoderia… · 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 Q0B6Q2
- Elsewhere: RCSB PDB 4GXW · PDBe 4GXW · UniProt Q0B6Q2
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