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Human carbonic anhydrase II mutant T199V bound by 3-(cyclooctylamino)- 2,5,6-trifluoro-4-[(2-HYDROXYETHYL)SULFONYL]BENZENESULFONAMIDE

Analyse Human carbonic anhydrase II mutant T199V bound by 3-(cyclooctylamino)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RMY
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00918
Ligands: V14, BCN, ZN

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	258	—	P00918

Ligands and binding sites

V14 · 3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide · ligand · chains A
BCN · Bicine · ligand · chains A
ZN · Zinc ion · metal · chains A
DMS · Dimethyl sulfoxide · additive · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6RMY · Human Carbonic anhydrase II mutant T199V bound by… · 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 6RMY · PDBe 6RMY · UniProt P00918

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