Structure of PDB 3d68 Chain C Binding Site BS02

Receptor Information
>3d68 Chain C (length=401) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFV
NASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQ
YHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQTAKN
AIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPV
VNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSS
SCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSY
TRSKSKDHEELSLVASEAVRAIEKISKNIRYTYGQGSETLYLAPGGGDDW
IYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRN
V
Ligand information
Ligand IDARG
InChIInChI=1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/p+1/t4-/m0/s1
InChIKeyODKSFYDXXFIFQN-BYPYZUCNSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(C(=O)O)N)CNC(=[NH2+])N
CACTVS 3.341N[C@@H](CCCNC(N)=[NH2+])C(O)=O
OpenEye OEToolkits 1.5.0C(C[C@@H](C(=O)O)N)CNC(=[NH2+])N
CACTVS 3.341N[CH](CCCNC(N)=[NH2+])C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCN\C(=[NH2+])N
FormulaC6 H15 N4 O2
NameARGININE
ChEMBL
DrugBank
ZINC
PDB chain3d68 Chain C Residue 650 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3d68 Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation
Resolution2.8 Å
Binding residue
(original residue number in PDB)		H159 R217 N234 S299 D348 E363
Binding residue
(residue number reindexed from 1)		H159 R217 N234 S299 D348 E363
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H159 E162 R217 H288 E363
Catalytic site (residue number reindexed from 1) H159 E162 R217 H288 E363
Enzyme Commision number 3.4.17.20: carboxypeptidase U.
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0004181 metallocarboxypeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0003331 positive regulation of extracellular matrix constituent secretion
GO:0006508 proteolysis
GO:0007596 blood coagulation
GO:0009410 response to xenobiotic stimulus
GO:0010757 negative regulation of plasminogen activation
GO:0030163 protein catabolic process
GO:0042730 fibrinolysis
GO:0051918 negative regulation of fibrinolysis
GO:0071333 cellular response to glucose stimulus
GO:0097421 liver regeneration
GO:2000346 negative regulation of hepatocyte proliferation
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3d68, PDBe:3d68, PDBj:3d68
PDBsum3d68
PubMed18559974
UniProtQ96IY4|CBPB2_HUMAN Carboxypeptidase B2 (Gene Name=CPB2)

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