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5DLW

Crystal structure of Autotaxin (ENPP2) with tauroursodeoxycholic acid (TUDCA) and lysophosphatidic acid (LPA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001953biological_processnegative regulation of cell-matrix adhesion
A0003676molecular_functionnucleic acid binding
A0004528molecular_functionphosphodiesterase I activity
A0004622molecular_functionlysophospholipase activity
A0005044molecular_functionscavenger receptor activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006644biological_processphospholipid metabolic process
A0006935biological_processchemotaxis
A0006955biological_processimmune response
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0009395biological_processphospholipid catabolic process
A0010634biological_processpositive regulation of epithelial cell migration
A0016042biological_processlipid catabolic process
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0030149biological_processsphingolipid catabolic process
A0030247molecular_functionpolysaccharide binding
A0030334biological_processregulation of cell migration
A0034638biological_processphosphatidylcholine catabolic process
A0044849biological_processestrous cycle
A0046872molecular_functionmetal ion binding
A0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
A0048714biological_processpositive regulation of oligodendrocyte differentiation
A0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
A0051894biological_processpositive regulation of focal adhesion assembly
A0060326biological_processcell chemotaxis
A0071276biological_processcellular response to cadmium ion
A0071392biological_processcellular response to estradiol stimulus
A1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
A1903165biological_processresponse to polycyclic arene
A2000394biological_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
ACYS73-CYS93
ACYS117-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
ATHR209

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
AASP311
AHIS315
AHIS359
AHIS474
AASP171
ATHR209

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R1E6
ChainResidueDetails
ALEU243
APHE210

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:27075612, ECO:0007744|PDB:5DLW
ChainResidueDetails
AASN230

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:27075612, ECO:0007744|PDB:5DLV, ECO:0007744|PDB:5DLW
ChainResidueDetails
ATYR306

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
AASP358

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
APRO764

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
ATHR772
AHIS766
ATYR768

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
AILE770

site_idSWS_FT_FI10
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN398
AALA410
AASP610
AHIS831
AASN53

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21240271
ChainResidueDetails
AASN524

221051

PDB entries from 2024-06-12

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