Structure of PDB 6y0f Chain B

Receptor sequence
>6y0fB (length=719) Species: 9606 (Homo sapiens) [Search protein sequence]
MRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYT
ILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNG
EFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGR
ENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSY
YGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIAS
SDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEH
IEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAI
QITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKC
VTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKIL
EENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLI
QVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAV
YRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGT
GLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEY
FRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSG
LSTNHLYTHMTHFLKQCFS
3D structure
PDB6y0f Structure of human FAPalpha in complex with linagliptin
ChainB
Resolution2.924 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y541 S624 Y625 D702 H734
Catalytic site (residue number reindexed from 1) Y503 S586 Y587 D664 H696
Enzyme Commision number 3.4.14.5: dipeptidyl-peptidase IV.
3.4.21.-
3.4.21.26: prolyl oligopeptidase.
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 356 B E203 E204 Y541 W623 S624 Y625 Y656 Y660 E165 E166 Y503 W585 S586 Y587 Y618 Y622 BindingDB: IC50=89nM
Gene Ontology
Molecular Function
GO:0002020 protease binding
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005178 integrin binding
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0001525 angiogenesis
GO:0006508 proteolysis
GO:0006915 apoptotic process
GO:0007155 cell adhesion
GO:0010710 regulation of collagen catabolic process
GO:0010716 negative regulation of extracellular matrix disassembly
GO:0043542 endothelial cell migration
GO:0051603 proteolysis involved in protein catabolic process
GO:0051726 regulation of cell cycle
GO:0051917 regulation of fibrinolysis
GO:0060244 negative regulation of cell proliferation involved in contact inhibition
GO:0097325 melanocyte proliferation
GO:1900119 positive regulation of execution phase of apoptosis
GO:1902362 melanocyte apoptotic process
GO:1903054 negative regulation of extracellular matrix organization
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0005925 focal adhesion
GO:0009986 cell surface
GO:0016020 membrane
GO:0030027 lamellipodium
GO:0031258 lamellipodium membrane
GO:0032587 ruffle membrane
GO:0042995 cell projection
GO:0045177 apical part of cell
GO:0045178 basal part of cell
GO:0070161 anchoring junction
GO:1905368 peptidase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6y0f, PDBe:6y0f, PDBj:6y0f
PDBsum6y0f
PubMed
UniProtQ12884|SEPR_HUMAN Prolyl endopeptidase FAP (Gene Name=FAP)

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