Structure of PDB 8a7d Chain C Binding Site BS02

Receptor Information
>8a7d Chain C (length=921) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRALYFSGRGEQLRLRADLELPRDAFTLQVWLRAEGGQRSPAVITGLYDK
CSYISRDRGWVVGIHTISDQDNKDPRYFFSLKTDRARQVTTINAHRSYLP
GQWVYLAATYDGQFMKLYVNGAQVATSGEQVGGIFSPLTQKCKVLMLGGS
ALNHNYRGYIEHFSLWKVARTQREILSDMETHGAHTALPQLLLQENWDNV
KHAWSPMKDGSSPKVEFSNAHGFLLDTSLEPPLCGQTLCDNTEVIASYNQ
LSSFRQPKVVRYRVVNLYEDDHKNPTVTREQVDFQHHQLAEAFKQYNISW
ELDVLEVSNSSLRRRLILANCDISKIGDENCDPECNHTLTGHDGGDCRHL
RHPAFVKKQHNGVCDMDCNYERFNFDGGECCDPEITNVTQTCFDPDSPHR
AYLDVNELKNILKLDGSTHLNIFFAKSSEEELAGVATWPWDKEALMHLGG
IVLNPSFYGMPGHTHTMIHQIGHSLGLYHVFRGISEIQSCSDPCMETEPS
FETGDLCNDTNPAPKHKSCGDPGPGNDTCGFHSFFNTPYNNFMSYADDDC
TDSFTPNQVARMHCYLDLVYQGWQPSRKPAPVALAPQVLGHTTDSVTLEW
FPPIDGHFFERELGSACHLCLEGRILVQYASNASSPMPCSPSGHWSPREA
EGHPDVEQPCKSSVRTWSPNSAVNPHTVPPACPEPQGCYLELEFLYPLVP
ESLTIWVTFVSTDWDSSGAVNDIKLLAVSGKNISLGPQNVFCDVPLTIRL
WDVGEEVYGIQIYTLDEHLEIDAAMLTSTADTPLCLQCKPLKYKVVRDPP
LQMDVASILHLNRKFVDMDLNLGSVYQYWVITISGTEESEPSPAVTYIHG
SGYCGDGIIQKDQGEQCDDMNKINGDGCSLFCRQEVSFNCIDEPSRCYFH
DGDGVCEEFEQKTSIKDCGVY
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain8a7d Chain C Residue 1709 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8a7d Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism.
Resolution3.06 Å
Binding residue
(original residue number in PDB)		K418 D421 N423 D425 D436 D439
Binding residue
(residue number reindexed from 1)		K325 D328 N330 D332 D343 D346
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.24.79: pappalysin-1.
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0005515 protein binding
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007166 cell surface receptor signaling pathway
GO:0007565 female pregnancy
GO:0030163 protein catabolic process
GO:0032354 response to follicle-stimulating hormone
GO:0071548 response to dexamethasone
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8a7d, PDBe:8a7d, PDBj:8a7d
PDBsum8a7d
PubMed36257932
UniProtQ13219|PAPP1_HUMAN Pappalysin-1 (Gene Name=PAPPA)

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