MolNFT v1 · #46042 · protein
Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain
2NSM · Carboxypeptidase N catalytic chain: “Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain”. X-ray diffraction, 2 ligands (NAG, SO4), 2 pockets (best druggability 0.48). MolNFT v1 #46042 on GenesisL1: 3D…
- PDB
- 2NSM
- Type
- protein
- Length
- 390 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase N catalytic chain
- EC
- 3.4.17.3
- UniProt
- P15169
- Ligands
- NAG, SO4
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase N catalytic chain (EC 3.4.17.3) | protein | 390 | 35% helix, 25% strand | P15169 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.48 | 0.84 | 25 | SO4 |
| 2 | 106 | 0.41 | 0.77 | 20 | empty |
Modifications
Observed in the structure: 3 glycan, 2 disulfide (O-glycosylation, disulfide).
Compared structures
- 2NSM · Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
- P15169 · AlphaFold monomer V2.0 prediction for carboxypeptidase N catalytic chain (P15169) · a predicted model of the same protein · 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 P15169
- Elsewhere: RCSB PDB 2NSM · PDBe 2NSM · UniProt P15169
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