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The structure of human carbonic anhydrase II in complex with bromide and azide

Analyse The structure of human carbonic anhydrase II in complex with bromide and azide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RAZ
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase II
EC: 4.2.1.1
UniProt: P00918
Ligands: ZN, BR
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase II (EC 4.2.1.1)	protein	258	17% helix, 31% strand	P00918

Ligands and binding sites

ZN · Zinc ion · metal · chains A
BR · Bromide ion · ion · 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	110	0.53	0.82	22	BR
2	56	0.28	0.74	13	empty

Compared structures

1RAZ · The structure of human carbonic anhydrase II in complex with bromide and azide · the same entry in another collection · chain A against A, TM-score 1.00
P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 1RAZ · PDBe 1RAZ · UniProt P00918

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