Research workbench
AlphaFold monomer V2.0 prediction for murein tetrapeptide carboxypeptidase (P76008)
Analyse AlphaFold monomer V2.0 prediction for murein tetrapeptide carboxypeptidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P76008
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- UniProt
- P76008
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 304 | — | P76008 |
Compared structures
- 5Z01 · Native Escherichia coli L,D-carboxypeptidase A (LdcA) · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 5Z01 · Native escherichia COLI L,D-carboxypeptidase a (ldca) · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 5Z03 · Mutant (S106A) escherichia COLI L,D-carboxypeptidase a (ldca) · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 5Z03 · Mutant (S106A) Escherichia coli L,D-carboxypeptidase A (LdcA) · an experimental structure of the same protein · chain A against B, TM-score 0.92
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 P76008
- Elsewhere: UniProt P76008 · AlphaFold DB P76008
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