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Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

Analyse Structural and kinetic analysis of proton shuttle residues in the active site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HFW
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase 3
EC: 4.2.1.1
UniProt: P07451
Ligands: ZN
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase 3 (EC 4.2.1.1)	protein	257	16% helix, 30% strand	P07451

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

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	173	0.51	0.78	27	ZN

Compared structures

2HFW · Structural and kinetic analysis of proton shuttle residues in the active site of human… · the same entry in another collection · chain A against A, TM-score 1.00
P07451 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 3 (P07451) · 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 P07451
Elsewhere: RCSB PDB 2HFW · PDBe 2HFW · UniProt P07451

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