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Crystal structure of D-alanine carboxypeptidase ampc from burkholderia cenocepacia
Analyse Crystal structure of D-alanine carboxypeptidase ampc from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E2G
- Type
- protein
- Length
- 694 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B4EPS2
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 349 | — | B4EPS2 |
| B | — | protein | 345 | — | B4EPS2 |
Compared structures
- 5E2G · Crystal Structure of D-alanine Carboxypeptidase AmpC from Burkholderia cenocepacia · 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 B4EPS2
- Elsewhere: RCSB PDB 5E2G · PDBe 5E2G · UniProt B4EPS2
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