Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1Z68

Crystal Structure Of Human Fibroblast Activation Protein alpha

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0002020molecular_functionprotease binding
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0007155biological_processcell adhesion
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0008239molecular_functiondipeptidyl-peptidase activity
A0009986cellular_componentcell surface
A0010710biological_processregulation of collagen catabolic process
A0010716biological_processnegative regulation of extracellular matrix disassembly
A0016020cellular_componentmembrane
A0030027cellular_componentlamellipodium
A0031258cellular_componentlamellipodium membrane
A0032587cellular_componentruffle membrane
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042995cellular_componentcell projection
A0043542biological_processendothelial cell migration
A0045177cellular_componentapical part of cell
A0045178cellular_componentbasal part of cell
A0051603biological_processproteolysis involved in protein catabolic process
A0051726biological_processregulation of cell cycle
A0051917biological_processregulation of fibrinolysis
A0060244biological_processnegative regulation of cell proliferation involved in contact inhibition
A0070161cellular_componentanchoring junction
A0097325biological_processmelanocyte proliferation
A1900119biological_processpositive regulation of execution phase of apoptosis
A1902362biological_processmelanocyte apoptotic process
A1903054biological_processnegative regulation of extracellular matrix organization
A1905368cellular_componentpeptidase complex
B0001525biological_processangiogenesis
B0002020molecular_functionprotease binding
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0007155biological_processcell adhesion
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0009986cellular_componentcell surface
B0010710biological_processregulation of collagen catabolic process
B0010716biological_processnegative regulation of extracellular matrix disassembly
B0016020cellular_componentmembrane
B0030027cellular_componentlamellipodium
B0031258cellular_componentlamellipodium membrane
B0032587cellular_componentruffle membrane
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042995cellular_componentcell projection
B0043542biological_processendothelial cell migration
B0045177cellular_componentapical part of cell
B0045178cellular_componentbasal part of cell
B0051603biological_processproteolysis involved in protein catabolic process
B0051726biological_processregulation of cell cycle
B0051917biological_processregulation of fibrinolysis
B0060244biological_processnegative regulation of cell proliferation involved in contact inhibition
B0070161cellular_componentanchoring junction
B0097325biological_processmelanocyte proliferation
B1900119biological_processpositive regulation of execution phase of apoptosis
B1902362biological_processmelanocyte apoptotic process
B1903054biological_processnegative regulation of extracellular matrix organization
B1905368cellular_componentpeptidase complex
Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqitAvrkFiemgfidekriaiwGwSyGGYV
ChainResidueDetails
AASP599-VAL629

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:15809306
ChainResidueDetails
ASER624
BSER624

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:15809306
ChainResidueDetails
AASP702
AHIS734
BASP702
BHIS734

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:15809306
ChainResidueDetails
AGLU203
AGLU204
BGLU203
BGLU204

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:15809306
ChainResidueDetails
AASN49
AASN92
AASN314
BASN49
BASN92
BASN314

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN99
BASN99

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:15809306, ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN227
BASN227

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN679
BASN679

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
AASP702
AHIS734
ASER624

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
BASP702
BHIS734
BSER624

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
AHIS734
ASER624
AASP703

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
BHIS734
BSER624
BASP703

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon