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Crystal structure of putative carboxypeptidase (YP_103406.1) from burkholderia mallei atcc 23344 at 2.49 a resolution
Analyse Crystal structure of putative carboxypeptidase (YP_103406.1) from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K2K
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative carboxypeptidase
- UniProt
- Q62IR3
- Ligands
- CL
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative carboxypeptidase | protein | 387 | 31% helix, 23% strand | Q62IR3 |
Ligands and binding sites
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 | 173 | 0.65 | 0.86 | 35 | CL |
| 2 | 52 | 0.43 | 0.83 | 22 | GOL |
| 3 | 56 | 0.33 | 0.77 | 14 | empty |
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 3K2K · Crystal structure of putative carboxypeptidase (YP_103406.1) from BURKHOLDERIA MALLEI… · 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 Q62IR3
- Elsewhere: RCSB PDB 3K2K · PDBe 3K2K · UniProt Q62IR3
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