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1S18

Structure and protein design of human apyrase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0017110molecular_functionnucleoside diphosphate phosphatase activity
B0005509molecular_functioncalcium ion binding
B0017110molecular_functionnucleoside diphosphate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
ASER98
AASP99
AGLU145
AGLU214
ASER275
AGLU326
AHOH3135

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BGLU145
BGLU214
BSER275
BGLU326
BHOH3020
BSER98
BASP99

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 3001
ChainResidue
AGLN234

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 3002
ChainResidue
BLYS161
BGLU162
BTRP163
BTHR164

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B 3003
ChainResidue
BASP133
BLYS143
BTRP163
BASN174
BPRO175
BHOH3046
BHOH3136
BHOH3235

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 3004
ChainResidue
BARG93
BARG113
BLYS143
BTRP163
BHOH3220
BHOH3239

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 2001
ChainResidue
ATYR21
AILE101
AVAL102
AVAL149
ALYS278
AGLU329
AHOH3016
AHOH3026
AHOH3145
AHOH3270

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS A 2002
ChainResidue
ALEU23
ALEU59
ALYS61
AILE120
AGLU121
AGLY122
AHOH3177
BTYR63
BTRS2007

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS B 2003
ChainResidue
BTYR21
BVAL102
BLYS278
BGLU329
BHOH3019
BHOH3032
BHOH3103
BHOH3112
BHOH3169
BHOH3185

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS B 2004
ChainResidue
ATYR63
BLEU23
BLEU59
BLYS61
BILE120
BGLU121
BGLY122
BTRS2007
BHOH3098
BHOH3237

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 2005
ChainResidue
AILE260
AALA261
AVAL262
AHOH3021
AHOH3106
AHOH3113
AHOH3141
BALA232
BSER233
BGLN234
BLYS245

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS B 2006
ChainResidue
AARG236
BVAL262
BSER263
BHIS264

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS B 2007
ChainResidue
AARG36
ALYS61
ATRS2002
BARG36
BLYS61
BTRS2004
BHOH3195
BHOH3237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:16835225, ECO:0007744|PDB:1S18, ECO:0007744|PDB:1S1D, ECO:0007744|PDB:2H2N, ECO:0007744|PDB:2H2U
ChainResidueDetails
ASER98
AGLU145
AGLU214
ASER275
AGLU326
BSER98
BGLU145
BGLU214
BSER275
BGLU326

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:16835225, ECO:0007744|PDB:1S18, ECO:0007744|PDB:2H2N, ECO:0007744|PDB:2H2U
ChainResidueDetails
AASP99
BASP99

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Important for dimer formation => ECO:0000269|PubMed:16835225
ChainResidueDetails
AGLU90
AILE130
ASER132
ASER186
BGLU90
BILE130
BSER132
BSER186

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN18
BASN18

219869

PDB entries from 2024-05-15

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