MolNFT v1 · #29456 · protein

Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer.

1Z97: “Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer.”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.61). MolNFT v1 #29456 on GenesisL1: 3D structure, binding sites and…

PDB: 1Z97
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase III
EC: 4.2.1.1
UniProt: P07451
Ligands: ZN
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase III (EC 4.2.1.1)	protein	263	16% helix, 29% strand	P07451

Ligands and binding sites

ZN · Zinc ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	171	0.61	0.83	25	empty
2	52	0.27	0.74	12	empty

Compared structures

1Z97 · Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton… · the same entry in another collection · chain A against A, TM-score 1.00
P07451 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 3 (P07451) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P07451
Elsewhere: RCSB PDB 1Z97 · PDBe 1Z97 · UniProt P07451

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