Structure of PDB 4aqd Chain A

Receptor sequence
>4aqdA (length=527) Species: 9606 (Homo sapiens) [Search protein sequence]
DIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKW
SDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAP
KPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAA
SVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGC
SRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDM
PDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQE
GLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPA
LEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLT
LNTESTRIMTKLRAQQCRFWTSFFPKV
3D structure
PDB4aqd Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G116 G117 G149 S198 A199 Y237 V288 F290 E325 H438
Catalytic site (residue number reindexed from 1) G114 G115 G147 S196 A197 Y235 V286 F288 E323 H436
Enzyme Commision number 3.1.1.8: cholinesterase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FUL A N245 F278 N243 F276
BS02 FUL A S487 T488 T508 S485 T486 T506
BS03 BAL A G116 G117 S198 A199 H438 G114 G115 S196 A197 H436
BS04 GLY A D129 K131 D127 K129
Gene Ontology
Molecular Function
GO:0004104 cholinesterase activity

View graph for
Molecular Function
External links
PDB RCSB:4aqd, PDBe:4aqd, PDBj:4aqd
PDBsum4aqd
PubMed22726956
UniProtP06276|CHLE_HUMAN Cholinesterase (Gene Name=BCHE)

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