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Crystal structure of human carbonic anhydrase I in complex with 4-(3- (2-((2-FLUOROBENZYL)AMINO)ETHYL)UREIDO) benzenesulfonamide

Analyse Crystal structure of human carbonic anhydrase I in complex with 4-(3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XZY
Type: protein
Length: 514 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00915
Ligands: O5N, ZN

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	257	—	P00915

Ligands and binding sites

O5N · 1-[2-[(2-fluorophenyl)methylamino]ethyl]-3-(3-sulfamoylphenyl)urea · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B

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

Compared structures

6XZY · crystal structure of human carbonic anhydrase I in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P00915 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 1 (P00915) · 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 P00915
Elsewhere: RCSB PDB 6XZY · PDBe 6XZY · UniProt P00915

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