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6FZB

AadA in complex with ATP, magnesium and streptomycin

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 Residues10
Detailsbinding site for residue SRY A 301
ChainResidue
AGLU87
AHOH411
ATRP112
AASP130
ATRP173
AALA177
AASP178
AASP182
AHIS185
AATP304

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AASP47
AASP49
AMG303
AATP304
AHOH407

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 303
ChainResidue
AASP47
AASP49
AGLU87
AMG302
AATP304
AHOH425

site_idAC4
Number of Residues25
Detailsbinding site for residue ATP A 304
ChainResidue
ASER36
AGLY41
ASER46
AASP47
AASP49
AASP130
ALEU133
ALEU134
AGLN137
AARG192
AILE193
ATHR196
APHE202
ALYS205
ATYR231
ASRY301
AMG302
AMG303
AHOH407
AHOH422
AHOH448
AHOH457
AHOH460
AHOH480
AHOH483

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
BGLY41
BLEU42
BPHE252

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 306
ChainResidue
AGLY41
ALEU42
APHE252
AHOH440

site_idAC7
Number of Residues4
Detailsbinding site for residue PEG A 307
ChainResidue
AGLU151
AARG152
APHE154
ATHR155

site_idAC8
Number of Residues4
Detailsbinding site for residue PEG A 308
ChainResidue
BGLU151
BARG152
BLEU153
BTHR155

site_idAC9
Number of Residues10
Detailsbinding site for residue SRY B 301
ChainResidue
BGLU87
BTRP112
BASP130
BTRP173
BALA177
BASP178
BASP182
BHIS185
BATP304
BHOH439

site_idAD1
Number of Residues5
Detailsbinding site for residue MG B 302
ChainResidue
BASP47
BASP49
BMG303
BATP304
BHOH405

site_idAD2
Number of Residues5
Detailsbinding site for residue MG B 303
ChainResidue
BASP47
BASP49
BGLU87
BMG302
BATP304

site_idAD3
Number of Residues26
Detailsbinding site for residue ATP B 304
ChainResidue
BMG303
BHOH405
BHOH422
BHOH438
BHOH447
BHOH459
BHOH470
BHOH472
BSER36
BGLY41
BSER46
BASP47
BASP49
BASP130
BLEU133
BLEU134
BGLN137
BLEU166
BARG192
BILE193
BTHR196
BPHE202
BLYS205
BTYR231
BSRY301
BMG302

site_idAD4
Number of Residues13
Detailsbinding site for residue GOL B 305
ChainResidue
AALA15
AALA15
AARG18
AARG18
AARG22
AARG22
BALA15
BALA15
BARG18
BARG18
BLEU19
BARG22
BARG22

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
AGLU87
BGLU87

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
BGLU87
BASP130
BLYS205
BTYR231
ASER46
AASP47
AASP49
AGLU87
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 2024-07-10

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