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8C4W

Crystal structure of rat autotaxin and compound MEY-002

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005044molecular_functionscavenger receptor activity
A0006955biological_processimmune response
A0016787molecular_functionhydrolase activity
A0030247molecular_functionpolysaccharide binding
A0046872molecular_functionmetal ion binding
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
AASP171
ATHR209
AASP311
AHIS315
AHIS359
AHIS474

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R1E6
ChainResidueDetails
AASN230

site_idSWS_FT_FI4
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_FI5
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_FI6
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
AHIS766
ATYR768
ATHR772

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:5IJS, ECO:0007744|PDB:5L0K
ChainResidueDetails
AILE770

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Essential for catalytic activity => ECO:0000250|UniProtKB:Q9R1E6
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AALA53
AASN398
AALA410
AASP610
AHIS831

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21240271
ChainResidueDetails
AASN524

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PDB entries from 2024-11-06

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