MolNFT v1 · #29915 · protein
Human carbonic anhydrase IV
1ZNC: “Human carbonic anhydrase IV”. X-ray diffraction, 2 ligands (ZN, SO4), 6 pockets (best druggability 0.70). MolNFT v1 #29915 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZNC
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase IV
- EC
- 4.2.1.1
- UniProt
- P22748
- Ligands
- ZN, SO4
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase IV (EC 4.2.1.1) | protein | 262 | 16% helix, 32% strand | P22748 |
| B | Carbonic anhydrase IV (EC 4.2.1.1) | protein | 247 | 17% helix, 33% strand | P22748 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 883 | 0.70 | 0.75 | 85 | empty |
| 2 | 130 | 0.52 | 0.80 | 22 | SO4, ZN |
| 3 | 147 | 0.51 | 0.79 | 23 | ZN, SO4 |
| 4 | 69 | 0.39 | 0.79 | 17 | empty |
| 5 | 77 | 0.37 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 415 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (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 P22748
- Elsewhere: RCSB PDB 1ZNC · PDBe 1ZNC · UniProt P22748
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