MolNFT v1 · #112805 · protein

Surface lysine acetylated human carbonic anhydrase II in complex with a sulfamate-based inhibitor

4ZWI · Carbonic anhydrase 2: “Surface lysine acetylated human carbonic anhydrase II in complex with a sulfamate-based inhibitor”. X-ray diffraction, 2 ligands (62I, ZN), 1 pocket (best druggability 0.58). MolNFT v1 #112805 on GenesisL1: 3D…

PDB: 4ZWI
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase 2
EC: 4.2.1.1
UniProt: P00918
Ligands: 62I, ZN
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase 2 (EC 4.2.1.1)	protein	257	15% helix, 30% strand	P00918

Ligands and binding sites

62I · (6R)-1-O-acetyl-2,6-anhydro-6-{[4-(sulfamoyloxy) piperidin-1-yl]sulfonyl}-L-glucitol · ligand · chains A
ZN · Zinc ion · metal · chains A
DMS · Dimethyl sulfoxide · additive · 7 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.58	0.83	27	62I

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · 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 P00918
Elsewhere: RCSB PDB 4ZWI · PDBe 4ZWI · UniProt P00918

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