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Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II (N62A)

Analyse Role of hydrophilic residues in proton transfer during catalysis by human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DV7
Type: protein
Length: 258 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: ZN
Pockets: 2 · best druggability 0.54

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	258	15% helix, 30% strand	P00918

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	127	0.54	0.82	25	empty
2	68	0.29	0.74	15	empty

Compared structures

3DV7 · Role of Hydrophilic Residues in Proton Transfer During Catalysis by Human Carbonic… · 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 3DV7 · PDBe 3DV7 · UniProt P00918

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