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5LPA

AadA E87Q in complex with ATP, calcium and dihydrostreptomycin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0009012molecular_functionaminoglycoside 3''-adenylyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0070566molecular_functionadenylyltransferase activity
B0005524molecular_functionATP binding
B0009012molecular_functionaminoglycoside 3''-adenylyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0070566molecular_functionadenylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue ATP A 301
ChainResidue
ASER36
AHIS185
AARG192
AILE193
ATHR196
APHE202
ALYS205
ATYR231
A71R302
ACA303
ACA305
AGLY41
AHOH411
AHOH468
AHOH528
AHOH547
AHOH560
AHOH569
AHOH574
AHOH582
AHOH594
ASER46
AASP47
AASP49
AASP130
ALEU133
AGLN137
ALEU166

site_idAC2
Number of Residues18
Detailsbinding site for residue 71R A 302
ChainResidue
AGLN87
ATRP112
ATRP173
AALA177
AASP178
AASP182
AHIS185
AATP301
AHOH411
AHOH413
AHOH431
AHOH439
AHOH448
AHOH472
AHOH508
AHOH517
AHOH524
AHOH571

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 303
ChainResidue
AASP47
AASP49
AATP301
ACA305
AHOH454

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 304
ChainResidue
AGLY41
ALEU42
APHE252

site_idAC5
Number of Residues7
Detailsbinding site for residue CA A 305
ChainResidue
AASP47
AASP49
AGLN87
AATP301
ACA303
AHOH411
AHOH583

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 306
ChainResidue
ALEU3
AGLU140
ATHR141
APRO214
ALEU216
APRO217
AHOH603

site_idAC7
Number of Residues28
Detailsbinding site for residue ATP B 301
ChainResidue
BSER36
BGLY41
BSER46
BASP47
BASP49
BASP130
BLEU133
BGLN137
BLEU166
BHIS185
BARG192
BILE193
BTHR196
BPHE202
BLYS205
BTYR231
B71R302
BCA303
BCA306
BHOH416
BHOH455
BHOH524
BHOH539
BHOH549
BHOH570
BHOH591
BHOH593
BHOH605

site_idAC8
Number of Residues19
Detailsbinding site for residue 71R B 302
ChainResidue
BTRP173
BALA177
BASP178
BASP182
BHIS185
BATP301
BHOH416
BHOH418
BHOH446
BHOH464
BHOH472
BHOH474
BHOH528
BHOH535
BHOH586
BHOH593
BGLN87
BGLN108
BTRP112

site_idAC9
Number of Residues5
Detailsbinding site for residue CA B 303
ChainResidue
BASP47
BASP49
BATP301
BCA306
BHOH468

site_idAD1
Number of Residues3
Detailsbinding site for residue CL B 304
ChainResidue
BGLY41
BLEU42
BPHE252

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO B 305
ChainResidue
BGLU140
BTHR141
BPRO214
BLEU216
BPRO217
BHOH417
BHOH508

site_idAD3
Number of Residues7
Detailsbinding site for residue CA B 306
ChainResidue
BASP47
BASP49
BGLN87
BATP301
BCA303
BHOH416
BHOH571

site_idAD4
Number of Residues10
Detailsbinding site for residue EDO B 307
ChainResidue
ASER8
AGLU82
AHOH455
AHOH461
BSER8
BGLU82
BHOH414
BHOH421
BHOH425
BHOH459

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26527143, ECO:0000305|PubMed:29871922
ChainResidueDetails
AGLN87
BGLN87

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:29871922, ECO:0007744|PDB:5G4A, ECO:0007744|PDB:5LPA, ECO:0007744|PDB:5LUH, ECO:0007744|PDB:6FZB
ChainResidueDetails
ASER36
BSER46
BASP47
BASP49
BGLN87
BASP130
BLYS205
BTYR231
ASER46
AASP47
AASP49
AGLN87
AASP130
ALYS205
ATYR231
BSER36

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29871922, ECO:0007744|PDB:5LPA, ECO:0007744|PDB:5LUH, ECO:0007744|PDB:6FZB
ChainResidueDetails
ATRP173
BTRP173

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29871922, ECO:0007744|PDB:5LPA, ECO:0007744|PDB:5LUH
ChainResidueDetails
AHIS185
BHIS185

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PDB entries from 2024-10-09

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