MolNFT v1 · #19523 · protein
Duck carboxypeptidase D domain II
1QMU · Carboxypeptidase GP180 residues 503-882: “Duck carboxypeptidase D domain II”. X-ray diffraction, 4 ligands (NAG, MAN, ZN), 3 pockets (best druggability 0.52). MolNFT v1 #19523 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1QMU
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase GP180 residues 503-882
- UniProt
- Q90240
- Ligands
- NAG, MAN, ZN, SO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase GP180 residues 503-882 | protein | 380 | 28% helix, 26% strand | Q90240 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
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 | 69 | 0.52 | 0.86 | 21 | SO4, ZN |
| 2 | 73 | 0.44 | 0.81 | 22 | empty |
| 3 | 83 | 0.37 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 3 glycan, 1 disulfide (N-glycosylation, disulfide).
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 Q90240
- Elsewhere: RCSB PDB 1QMU · PDBe 1QMU · UniProt Q90240
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