Structure of PDB 8hgh Chain A

Receptor sequence
>8hghA (length=1462) Species: 9606,83333 [Search protein sequence]
PSRALYFSGRGEQLRLRADLELPRDAFTLQVWLRAEGGQRSPAVITGLYD
KCSYISRDRGWVVGIHTISDQDNKDPRYFFSLKTDRARQVTTINAHRSYL
PGQWVYLAATYDGQFMKLYVNGAQVATSGEQVGGIFSPLTQKCKVLMLGG
SALNHNYRGYIEHFSLWKVARTQREILSDMETHGAHTALPQLLLQENWDN
VKHAWSPMKDGSSPKVEFSNAHGFLLDTSLEPPLCGQTLCDNTEVIASYN
QLSSFRQPKVVRYRVVNLYEDDHKNPTVTREQVDFQHHQLAEAFKQYNIS
WELDVLEVSNSSLRRRLILANCDISKIGDENCDPECNHTLTGHDGGDCRH
LRDMDCNYEDGGECCDPEITNVTQTCFDPDSPHRAYLDVNELKNILKLDG
STHLNIFFAKSSEEELAGVATWPWDKEALMHLGGIVLNPSFYGMPGHTHT
MIHEIGHSLGLYHVFRGISEIQSCSDPCMETEPSFETGDLCNDTNPAPKH
KSCGDPGPGNDTCGFHSFFNTPYNNFMSYADDDCTDSFTPNQVARMHCYL
DLVYQGWQPSRKPAPVALAPQVLGHTTDSVTLEWFPPIDGHFFERELGSA
CHLCLEGRILVQYASNASSPMPCSPSGHWSPREAEGHPDVEQPCKSSVRT
WSPNSAVNPHTVPPACPEPQGCYLELEFLYPLVPESLTIWVTFVSTDWDS
SGAVNDIKLLAVSGKNISLGPQNVFCDVPLTIRLWDVGEEVYGIQIYTLD
EHLEIDAAMLTSTADTPLCLQCKPLKYKVVRDPPLQMDVASILHLNRKFV
DMDLNLGSVYQYWVITISGTEESEPSPAVTYIHGSGYCGDGIIQKDQGEQ
CDDMNKINGDGCSLFCRQEVSFNCIDEPSRCYFHDGDGVCEEFEQKTSIK
DCGVYTPQGFLDQWASNASVSHQDQQCPGWVIIGQPAASQVCRTKVIDLS
EGISQHAWYPCTISYPYSQLAQTTFWLRAYFSQPMVAAAVIVHLVTDGTY
YGDQKQETISVQLLDTKDQSHDLGLHVLSCRNNPLIIPVVHDLSQPFYHS
QAVRVSFSSPLVAISGVALRSFDNFDPVTLSSDCPELAVENASLNCSSSD
RYHGAQCTVSCRTGYVLQIRRDDELIKSQTGPSVTVTCTEGKWNKQVACE
PVDCSIPDHHQVYAASFSCPEGTTFGSQCSFQCRHPAQLKGNNSLLTCME
DGLWSFPEALCELMCLAPPPVPNADLQTARCRENKHKVGSFCKYKCKPGY
HVPGSSRKSKKRAFKTQCTQDGSWQEGACVPVTCDPPPPKFHGLYQCTNG
FQFNSECRIKLGSNVIHCRKDGTWNGSFHVNSNLKLQCPDGYAIGSECAT
SCLDHNSESIILPMNVTVRDIPHWLNPTRVERVVCTAGLKWYPHPALIHC
VKGCEPFMGDNYCDAINNRAFCNYDGGDCCTSTVKTKKVTPFPMSCDLQG
DCACRDPQAQEH
3D structure
PDB8hgh Structural insights into the covalent regulation of PAPP-A activity by proMBP and STC2.
ChainA
Resolution4.16 Å
3D
structure
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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 ZN A H482 H486 H492 H453 H457 H463
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:0015144 carbohydrate transmembrane transporter activity
GO:0046872 metal ion binding
GO:1901982 maltose binding
Biological Process
GO:0006508 proteolysis
GO:0006974 DNA damage response
GO:0007166 cell surface receptor signaling pathway
GO:0007565 female pregnancy
GO:0008643 carbohydrate transport
GO:0015768 maltose transport
GO:0030163 protein catabolic process
GO:0032354 response to follicle-stimulating hormone
GO:0034219 carbohydrate transmembrane transport
GO:0034289 detection of maltose stimulus
GO:0042956 maltodextrin transmembrane transport
GO:0055085 transmembrane transport
GO:0060326 cell chemotaxis
GO:0071548 response to dexamethasone
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0016020 membrane
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space
GO:0043190 ATP-binding cassette (ABC) transporter complex
GO:0055052 ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
GO:1990060 maltose transport complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8hgh, PDBe:8hgh, PDBj:8hgh
PDBsum8hgh
PubMed36550107
UniProtP0AEX9|MALE_ECOLI Maltose/maltodextrin-binding periplasmic protein (Gene Name=malE);
Q13219|PAPP1_HUMAN Pappalysin-1 (Gene Name=PAPPA)

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