Structure of PDB 8a7d Chain Q

Receptor sequence
>8a7dQ (length=273) Species: 9606 (Homo sapiens) [Search protein sequence]
PVDCSIPDHHQVYAASFSCPEGTTFGSQCSFQCRHPAQLKGNNSLLTCME
DGLWSFPEALCELMCLAPPPVPNADLQTARCRENKHKVGSFCKYKCKPGY
HVPGSSRKSKKRAFKTQCTQDGSWQEGACVPGQCSVPNELNSNLKLQCPD
GYAIGSECATSCLDHNSESIILPMNVTVRDIPHWLNPTRVERVVCTAGLK
WYPHPALIHCVKGCEPFMGDNYCDAINNRAFCNYDGGDCCTSTVKTKKVT
PFPMSCDLQGDCACRDPQAQEHS
3D structure
PDB8a7d Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism.
ChainQ
Resolution3.06 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.4.24.79: pappalysin-1.
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 CA Q F1561 M1562 D1564 Y1566 D1568 D1579 D1582 F217 M218 D220 Y222 D224 D235 D238
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

View graph for
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)

[Back to BioLiP]