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1S1D

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
AHOH5158

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BGLU214
BSER275
BGLU326
BHOH5041
BSER98
BGLU145

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 2001
ChainResidue
AASP133
ALYS143
AASN172
AASN174

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 3001
ChainResidue
BLYS60
BHIS81
BTYR325
BHOH5314

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 3002
ChainResidue
BARG113
BLYS143
BTRP163
BTRS5006
BHOH5216
BHOH5269

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GP2 A 4001
ChainResidue
AASP42
AASP44
AASP112
AGLU145
ALYS161
AGLU162
ATRP163
ATHR164
ATYR237
AASP242
ALYS324
AGLU326
AHOH5169
AHOH5275
AHOH5309
AHOH5336

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GP2 B 4002
ChainResidue
BASP42
BASP44
BLYS161
BGLU162
BTRP163
BTHR164
BGLU214
BARG230
BTYR237
BASP242
BGLU295
BLYS324
BGLU326
BHOH5055
BHOH5083
BHOH5140
BHOH5157
BHOH5322

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 5001
ChainResidue
ATYR21
AVAL102
AVAL149
ALYS278
AGLU329
AHOH5025
AHOH5026
AHOH5044
AHOH5091
AHOH5207
AHOH5295

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRS A 5002
ChainResidue
ALEU23
ALEU59
ALYS61
ALEU107
AILE120
AGLU121
AGLY122
AILE331
ATRS5007
AHOH5108
AHOH5142
BTYR63

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS B 5003
ChainResidue
BTYR21
BGLU329
BHOH5017
BHOH5019
BHOH5068
BHOH5070
BHOH5196

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS B 5004
ChainResidue
BILE331
BHOH5132
BHOH5144
ATYR63
ATRS5007
BLEU23
BLEU59
BLYS61
BLEU107
BILE120
BGLY122

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 5005
ChainResidue
AILE260
AALA261
AVAL262
AHOH5102
AHOH5298
AHOH5312
BALA232
BSER233
BGLN234
BLYS245
BHOH5089

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS B 5006
ChainResidue
BASP133
BLYS140
BLYS143
BTRP163
BASN172
BASN174
BPRO175
BSO43002
BHOH5020
BHOH5128
BHOH5134

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 5007
ChainResidue
AARG36
ALYS61
ATRS5002
AHOH5256
BARG36
BLYS61
BTRS5004
BHOH5185

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
BGLU326
AGLU145
AGLU214
ASER275
AGLU326
BSER98
BGLU145
BGLU214
BSER275

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

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PDB entries from 2024-07-17

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