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Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket of human carbonic anhydrase II

Analyse Structural consequences of hydrophilic amino-acid substitutions in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HEB
Type: protein
Length: 255 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, HG
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase II (EC 4.2.1.1)	protein	255	15% helix, 31% strand	P00918

Ligands and binding sites

ZN · Zinc ion · metal · chains A
HG · Mercury (II) ion · metal · 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	117	0.56	0.83	25	empty

Compared structures

1HEB · Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket… · 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 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 1HEB · PDBe 1HEB · UniProt P00918

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