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2B0Q

Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Neomycin B Complex

Replaces:  1L8U
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0008910molecular_functionkanamycin kinase activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NMY A 305
ChainResidue
AGLU24
AASP231
AASP261
AGLU262
APHE264
AHOH519
AHOH520
AGLU157
AASN158
AGLU160
AASP190
AASP193
ASER194
AARG226
AGLU230

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
ASER194
AASN195
AASP208
AADP300
AHOH519

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AASP190
AASP208
AADP300
AHOH520

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP A 300
ChainResidue
AASP22
AGLU24
AGLY25
ASER27
AVAL31
ATYR42
ALYS44
APRO74
AMET90
ASER91
AGLU92
AALA93
ALEU97
ASER194
AASN195
APHE197
AILE207
AASP208
AMG301
AMG302
AHOH519
AHOH520
AHOH544

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
DetailsAnnotated By Reference To The Literature 1l8t
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

237735

PDB entries from 2025-06-18

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