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1L8T

Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Kanamycin A Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0008910molecular_functionkanamycin kinase activity
A0016301molecular_functionkinase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AASN195
AASP208
AADP300
AHOH526
AHOH528

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AHOH562
AASP208
AADP300
AHOH527
AHOH539

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 300
ChainResidue
AASP22
AGLU24
AGLY25
AMET26
ASER27
ATYR42
ALYS44
AMET90
ASER91
AGLU92
AALA93
ALEU97
ASER194
AASN195
APHE197
AILE207
AASP208
AMG301
AMG302
AHOH521
AHOH526
AHOH527
AHOH528
AHOH535
AHOH536
AHOH564

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE KAN A 1
ChainResidue
AMET26
AGLU157
AASN158
AGLU160
AASP190
AARG226
ASER227
AGLU230
AASP261
AGLU262
APHE264
AHOH517
AHOH527
AHOH528
AHOH530
AHOH538
AHOH563
AHOH564

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP190

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9200607
ChainResidueDetails
ALYS44
AASP190

site_idMCSA1
Number of Residues4
DetailsM-CSA 640
ChainResidueDetails
ALYS44electrostatic stabiliser, polar interaction
AASP190proton acceptor, proton shuttle (general acid/base)
AASN195metal ligand
AASP208metal ligand

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PDB entries from 2024-11-06

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