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4GTW

Crystal structure of mouse Enpp1 in complex with AMP

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
B0003676molecular_functionnucleic acid binding
B0005044molecular_functionscavenger receptor activity
B0006955biological_processimmune response
B0016787molecular_functionhydrolase activity
B0030247molecular_functionpolysaccharide binding
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00524
Number of Residues21
DetailsSMB_1 Somatomedin B domain (SMB) signature. CrCdaaCvslgn.CClDFqetC
ChainResidueDetails
ACYS102-CYS122
ACYS146-CYS166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:23688339, ECO:0007744|PDB:3NKM, ECO:0007744|PDB:3NKN, ECO:0007744|PDB:3NKO, ECO:0007744|PDB:3NKP, ECO:0007744|PDB:3NKQ, ECO:0007744|PDB:3NKR, ECO:0007744|PDB:3WAV, ECO:0007744|PDB:3WAW, ECO:0007744|PDB:3WAX, ECO:0007744|PDB:3WAY, ECO:0007744|PDB:5INH
ChainResidueDetails
AASN53
BASN53

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: AMP-threonine intermediate => ECO:0000269|PubMed:11027689
ChainResidueDetails
ATHR238
BTHR238

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:30356045
ChainResidueDetails
AASP200
BASP405
BHIS406
BHIS517
AASP358
AHIS362
AASP405
AHIS406
AHIS517
BASP200
BASP358
BHIS362

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369
ChainResidueDetails
ATHR238
BGLY785
BTYR787
BSER789
APHE781
ATYR783
AGLY785
ATYR787
ASER789
BTHR238
BPHE781
BTYR783

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:23027977, ECO:0007744|PDB:4GTY
ChainResidueDetails
AASN259
ALEU272
ALYS277
ATYR322
BASN259
BLEU272
BLYS277
BTYR322

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:30356045
ChainResidueDetails
ASER514
BSER514

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Essential for catalytic activity => ECO:0000250|UniProtKB:Q9R1E6
ChainResidueDetails
ATHR896
BTHR896

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q924C3
ChainResidueDetails
ATHR238
BTHR238

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN161
BASN161

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23027977
ChainResidueDetails
AASN267
BASN267

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369
ChainResidueDetails
AASN323
BASN323

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23041369
ChainResidueDetails
AASN459
BASN459

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369
ChainResidueDetails
AASN567
BASN567

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23041369
ChainResidueDetails
AASN624
BASN624

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PDB entries from 2024-05-01

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