Research workbench

Ni- Carbonic Anhydrase II pH 11.0 0 atm CO2

Analyse Ni- Carbonic Anhydrase II pH 11.0 0 atm CO2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LV7
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.2
Source: Homo sapiens
Molecule: Carbonic anhydrase 2
EC: 4.2.1.1
UniProt: P00918
Ligands: NI
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · resolution 1.2 · 1 distinct chain · 16% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase 2 (EC 4.2.1.1)	protein	257	16% helix, 31% strand	P00918

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A
GOL · Glycerol · additive · 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	132	0.57	0.83	24	NI

Compared structures

6LV7 · Ni- carbonic anhydrase II pH 11.0 0 atm CO2 · 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 6LV7 · PDBe 6LV7 · UniProt P00918

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