MolNFT v1 · #47906 · protein
Human carboxypeptidase A4 in complex with a cleaved hexapeptide.
2PCU: “Human carboxypeptidase A4 in complex with a cleaved hexapeptide.”. X-ray diffraction, 4 ligands (ASP, NAG, ZN). MolNFT v1 #47906 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PCU
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase A4; Peptide
- EC
- 3.4.17.-
- UniProt
- Q9UI42
- Ligands
- ASP, NAG, ZN, SCN
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase A4 (EC 3.4.17.-) | protein | 305 | 39% helix, 17% strand | Q9UI42 |
| B | Peptide | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- ASP · Aspartic acid · ligand · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- ZN · Zinc ion · metal · chains A, B
- SCN · Thiocyanate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 391 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
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 Q9UI42
- Elsewhere: RCSB PDB 2PCU · PDBe 2PCU · UniProt Q9UI42
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