Structure of PDB 1q2l Chain A Binding Site BS01

Receptor Information
>1q2l Chain A (length=937) Species: 316407 (Escherichia coli str. K-12 substr. W3110) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVP
VGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTA
PYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMA
RTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHE
KYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDA
QKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSPGTL
SDWLQKQGLVEGISANSDPIVNGNSGVLAISASLTDKGLANRDQVVAAIF
SYLNLLREKGIDKQYFDELANVLDIDFRYPSITRDMDYVEWLADTMIRVP
VEHTLDAVNIADRYDAKAVKERLAMMTPQNARIWYISPKEPHNKTAYFVD
APYQVDKISAQTFADWQKKAADIALSLPELNPYIPDDFSLIKSEKKYDHP
ELIVDESNLRVVYAPSRYFASEPKADVSLILRNPKAMDSARNQVMFALND
YLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLFQALLEG
YFSYTATEDQLEQAKSWYNQMMDSAEKGKAFEQAIMPAQMLSQVPYFSRD
ERRKILPSITLKEVLAYRDALKSGARPEFMVIGNMTEAQATTLARDVQKQ
LGADGSEWCRNKDVVVDKKQSVIFEKAGNSTDSALAAVFVPTGYDEYTSS
AYSSLLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDK
QPSFLWERYKAFFPTAEAKLRAMKPDEFAQIQQAVITQMLQAPQTLGEEA
SKLSKDFDRGNMRFDSRDKIVAQIKLLTPQKLADFFHQAVVEPQGMAILS
QISGSQNGKAEYVHPEGWKVWENVSALQQTMPLMSEK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1q2l Chain A Residue 963 [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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PDB1q2l Crystal Structure of pitrilysin, the prototype of insulin-degrading enzymes
Resolution2.2 Å
Binding residue
(original residue number in PDB)		H88 H92 E169
Binding residue
(residue number reindexed from 1)		H65 H69 E146
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H88 E91 H92 E162 E169
Catalytic site (residue number reindexed from 1) H65 E68 H69 E139 E146
Enzyme Commision number 3.4.24.55: pitrilysin.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q2l, PDBe:1q2l, PDBj:1q2l
PDBsum1q2l
PubMed
UniProtP05458|PTRA_ECOLI Protease 3 (Gene Name=ptrA)

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