Structure of PDB 4qww Chain A Binding Site BS01

Receptor Information
>4qww Chain A (length=529) Species: 8613 (Bungarus fasciatus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AGELKVSTQTGSVRGLSLPVLDGHVSAFLGIPFAEPPLGRMRFLRPEPVK
PWQHVLDATSYKPACYQMVDTSYPGFQGTEMWNPNRGMSEDCLYLNIWVP
SPRPKDAPVLVWIYGGGFYSGAASLDVYDGRFLTYTQNVILVSLSYRVGA
FGFLGLPGSPEAPGNMGLLDQRLALQWIQNNIHPFGGNPRAVTVFGESAG
AASVGMHLLSTQSRTLFQRAILQSGGPNAPWATVTPAESRGRAALLGKQL
GCHFNNDSELVSCLRSKNPQELIDEEWSVLPYKSIFRFPFVPVIDGDFFP
DTPEAMLSSGNFKETQVLLGVVKDEGSYFLIYGLPGFSKDNESLISRADF
LEGVRMSVPHANDIATDAVVLQYTDWQDQDNREKNREALDDIVGDHNVIC
PVVQFANDYAKRNSKVYAYLFDHRASNLLWPPWMGVPHGYEIEFVFGLPL
NDSLNYTPQEKELSRRMMRYWANFARTGNPTDPAAWPTYTASQPQYVQLN
TQPLATQPSLRAQICAFWNHFLPKLLNAT
Ligand information
Ligand IDMAN
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5+,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-PQMKYFCFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@@H]1O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@@H]([C@H](O1)O)O)O)O)O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-mannopyranose;
alpha-D-mannose;
D-mannose;
mannose
ChEMBLCHEMBL365590
DrugBank
ZINCZINC000003860903
PDB chain4qww Chain H Residue 4 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4qww Crystal Structure of Snake Venom Acetylcholinesterase in Complex with Inhibitory Antibody Fragment Fab410 Bound at the Peripheral Site: EVIDENCE FOR OPEN AND CLOSED STATES OF A BACK DOOR CHANNEL.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		T61 S62
Binding residue
(residue number reindexed from 1)		T59 S60
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G118 G119 G151 S200 A201 A239 F290 F292 E327 H440
Catalytic site (residue number reindexed from 1) G116 G117 G149 S198 A199 A237 F288 F290 E325 H438
Enzyme Commision number 3.1.1.7: acetylcholinesterase.
Gene Ontology
Molecular Function
GO:0003990 acetylcholinesterase activity
GO:0004104 cholinesterase activity
GO:0052689 carboxylic ester hydrolase activity
GO:0090729 toxin activity
Biological Process
GO:0001507 acetylcholine catabolic process in synaptic cleft
GO:0006581 acetylcholine catabolic process
GO:0019695 choline metabolic process
GO:0035821 modulation of process of another organism
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0043083 synaptic cleft
GO:0045202 synapse

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4qww, PDBe:4qww, PDBj:4qww
PDBsum4qww
PubMed25411244
UniProtQ92035|ACES_BUNFA Acetylcholinesterase (Gene Name=ACHE)

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