Structure of PDB 4aqd Chain B

Receptor sequence
>4aqdB (length=526) Species: 9606 (Homo sapiens) [Search protein sequence]
IIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWS
DIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPK
PKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGF
LALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAAS
VSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCS
RENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMP
DILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEG
LKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPAL
EFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERR
DNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTL
NTESTRIMTKLRAQQCRFWTSFFPKV
3D structure
PDB4aqd Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure.
ChainB
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) G113 G114 G146 S195 A196 Y234 V285 F287 E322 H435
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 B N245 K248 L249 F278 N242 K245 L246 F275
BS02 BAL B G116 G117 S198 H438 G113 G114 S195 H435
BS03 GLY B L18 D129 K131 L15 D126 K128
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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