MolNFT v1 · #22735 · protein

Effect of shuttle location and pH environment on H+ transfer in human carbonic anhydrase II

1TEQ: “Effect of shuttle location and pH environment on H+ transfer in human carbonic anhydrase II”. X-ray diffraction, 2 ligands (ZN, OH), 2 pockets (best druggability 0.55). MolNFT v1 #22735 on GenesisL1: 3D structure, binding sites and…

PDB: 1TEQ
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, OH
Pockets: 2 · best druggability 0.55

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Carbonic anhydrase II (EC 4.2.1.1)	protein	258	16% helix, 30% strand	P00918

Ligands and binding sites

ZN · Zinc ion · metal · chains X
OH · Hydroxide ion · ion · chains X

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	129	0.55	0.82	28	OH
2	65	0.29	0.74	16	empty

Compared structures

1TEQ · Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase… · the same entry in another collection · chain X against X, TM-score 1.00
P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain X 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 1TEQ · PDBe 1TEQ · UniProt P00918

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