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7P0K

Crystal structure of Autotaxin (ENPP2) with 18F-labeled positron emission tomography ligand

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0001953biological_processnegative regulation of cell-matrix adhesion
AAA0003676molecular_functionnucleic acid binding
AAA0004528molecular_functionphosphodiesterase I activity
AAA0004622molecular_functionlysophospholipase activity
AAA0005509molecular_functioncalcium ion binding
AAA0005576cellular_componentextracellular region
AAA0005615cellular_componentextracellular space
AAA0006644biological_processphospholipid metabolic process
AAA0006935biological_processchemotaxis
AAA0008270molecular_functionzinc ion binding
AAA0008284biological_processpositive regulation of cell population proliferation
AAA0009395biological_processphospholipid catabolic process
AAA0010634biological_processpositive regulation of epithelial cell migration
AAA0016042biological_processlipid catabolic process
AAA0016192biological_processvesicle-mediated transport
AAA0016787molecular_functionhydrolase activity
AAA0016788molecular_functionhydrolase activity, acting on ester bonds
AAA0030149biological_processsphingolipid catabolic process
AAA0030334biological_processregulation of cell migration
AAA0034638biological_processphosphatidylcholine catabolic process
AAA0044849biological_processestrous cycle
AAA0046872molecular_functionmetal ion binding
AAA0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
AAA0048714biological_processpositive regulation of oligodendrocyte differentiation
AAA0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
AAA0051894biological_processpositive regulation of focal adhesion assembly
AAA0060326biological_processcell chemotaxis
AAA0071276biological_processcellular response to cadmium ion
AAA0071392biological_processcellular response to estradiol stimulus
AAA1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
AAA1903165biological_processresponse to polycyclic arene
AAA2000394biological_processpositive regulation of lamellipodium morphogenesis
Functional Information from PROSITE/UniProt
site_idPS00524
Number of Residues21
DetailsSMB_1 Somatomedin B domain (SMB) signature. CrCdnlCksyss.CChDFdelC
ChainResidueDetails
AAACYS73-CYS93
AAACYS117-CYS137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:27268273
ChainResidueDetails
AAATHR209

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E, ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ
ChainResidueDetails
AAAASP171
AAATHR209
AAAASP311
AAAHIS315
AAAHIS359
AAAVAL488

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R1E6
ChainResidueDetails
AAAPHE210
AAALEU243

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:27075612, ECO:0007744|PDB:5DLW
ChainResidueDetails
AAAASN230

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:27075612, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW
ChainResidueDetails
AAATYR306

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0000269|PubMed:27660691, ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0B, ECO:0007744|PDB:5L0E, ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ
ChainResidueDetails
AAAASP358

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ
ChainResidueDetails
AAAARG798

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0K, ECO:0007744|PDB:5LQQ
ChainResidueDetails
AAAASP800
AAAASP802
AAAASN806

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:27075612, ECO:0000269|PubMed:27268273, ECO:0007744|PDB:2XR9, ECO:0007744|PDB:2XRG, ECO:0007744|PDB:5DLT, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW, ECO:0007744|PDB:5IJQ, ECO:0007744|PDB:5IJS, ECO:0007744|PDB:5L0K
ChainResidueDetails
AAASER804

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AAATYR402
AAALYS414
AAAILE644

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21240271
ChainResidueDetails
AAATHR538

220113

PDB entries from 2024-05-22

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