4ZG7
Structural basis for inhibition of human autotaxin by four novel compounds
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0005509 | molecular_function | calcium ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006644 | biological_process | phospholipid metabolic process |
| A | 0006935 | biological_process | chemotaxis |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 | 0030334 | biological_process | regulation of cell migration |
| A | 0034638 | biological_process | phosphatidylcholine catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047391 | molecular_function | alkylglycerophosphoethanolamine phosphodiesterase activity |
| A | 0048870 | biological_process | cell motility |
| A | 0050731 | biological_process | positive regulation of peptidyl-tyrosine phosphorylation |
| 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. CrCdnlCksyts.CChDFdelC |
| Chain | Residue | Details |
| A | CYS74-CYS94 | |
| A | CYS118-CYS138 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q9R1E6 |
| Chain | Residue | Details |
| A | THR210 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:5KXA |
| Chain | Residue | Details |
| A | ASP172 | |
| A | THR210 | |
| A | ASP359 | |
| A | HIS360 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9R1E6 |
| Chain | Residue | Details |
| A | PHE211 | |
| A | LEU244 | |
| A | TYR307 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:26371182, ECO:0007744|PDB:4ZG7 |
| Chain | Residue | Details |
| A | ASN231 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA |
| Chain | Residue | Details |
| A | ASP312 | |
| A | HIS316 | |
| A | HIS475 | |
| A | ASP744 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA |
| Chain | Residue | Details |
| A | ASP740 | |
| A | ASP742 | |
| A | LEU746 | |
| A | ASP748 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Essential for catalytic activity => ECO:0000250|UniProtKB:Q9R1E6 |
| Chain | Residue | Details |
| A | LYS853 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ALA411 | |
| A | ASN807 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA |
| Chain | Residue | Details |
| A | ASN525 |
