MolNFT v1 · #24494 · protein
Crystal structure of human carboxypeptidase M
1UWY: “Crystal structure of human carboxypeptidase M”. X-ray diffraction, 2 ligands (NAG, ZN), 4 pockets (best druggability 0.65). MolNFT v1 #24494 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UWY
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase M
- EC
- 3.4.17.12
- UniProt
- P14384
- Ligands
- NAG, ZN
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase M (EC 3.4.17.12) | protein | 393 | 26% helix, 21% strand | P14384 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.65 | 0.82 | 41 | empty |
| 2 | 220 | 0.58 | 0.80 | 26 | empty |
| 3 | 172 | 0.52 | 0.79 | 21 | empty |
| 4 | 63 | 0.34 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 3 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 P14384
- Elsewhere: RCSB PDB 1UWY · PDBe 1UWY · UniProt P14384
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