5IJQ
Crystal structure of autotaxin (ENPP2) re-refined
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001953 | biological_process | negative regulation of cell-matrix adhesion |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004528 | molecular_function | phosphodiesterase I activity |
A | 0004622 | molecular_function | lysophospholipase activity |
A | 0004630 | molecular_function | phospholipase D activity |
A | 0005044 | molecular_function | scavenger receptor activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006644 | biological_process | phospholipid metabolic process |
A | 0006935 | biological_process | chemotaxis |
A | 0006955 | biological_process | immune response |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008284 | biological_process | positive regulation of cell population proliferation |
A | 0009395 | biological_process | phospholipid catabolic process |
A | 0010634 | biological_process | positive regulation of epithelial cell migration |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016192 | biological_process | vesicle-mediated transport |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0030149 | biological_process | sphingolipid catabolic process |
A | 0030247 | molecular_function | polysaccharide binding |
A | 0030334 | biological_process | regulation of cell migration |
A | 0034638 | biological_process | phosphatidylcholine catabolic process |
A | 0044849 | biological_process | estrous cycle |
A | 0046872 | molecular_function | metal ion binding |
A | 0047391 | molecular_function | alkylglycerophosphoethanolamine phosphodiesterase activity |
A | 0048714 | biological_process | positive regulation of oligodendrocyte differentiation |
A | 0050731 | biological_process | positive regulation of peptidyl-tyrosine phosphorylation |
A | 0051894 | biological_process | positive regulation of focal adhesion assembly |
A | 0060326 | biological_process | cell chemotaxis |
A | 0071276 | biological_process | cellular response to cadmium ion |
A | 0071392 | biological_process | cellular response to estradiol stimulus |
A | 1900026 | biological_process | positive regulation of substrate adhesion-dependent cell spreading |
A | 1903165 | biological_process | response to polycyclic arene |
A | 2000394 | biological_process | positive regulation of lamellipodium morphogenesis |
Functional Information from PROSITE/UniProt
site_id | PS00524 |
Number of Residues | 21 |
Details | SMB_1 Somatomedin B domain (SMB) signature. CrCdnlCksyss.CChDFdelC |
Chain | Residue | Details |
A | CYS73-CYS93 | |
A | CYS117-CYS137 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:12633853, ECO:0000269|PubMed:27268273 |
Chain | Residue | Details |
A | THR209 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ASP171 | |
A | THR209 | |
A | ASP311 | |
A | HIS315 | |
A | HIS359 | |
A | HIS474 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9R1E6 |
Chain | Residue | Details |
A | ASN230 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ASP358 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | PRO764 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | HIS766 | |
A | TYR768 | |
A | THR772 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ILE770 |
site_id | SWS_FT_FI8 |
Number of Residues | 5 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN53 | |
A | ASN398 | |
A | ALA410 | |
A | ASP610 | |
A | HIS831 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21240271 |
Chain | Residue | Details |
A | ASN524 |