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4FEX

Crystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, with substrate kanamycin and small molecule inhibitor tyrphostin AG1478

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0046677biological_processresponse to antibiotic
B0005524molecular_functionATP binding
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0046677biological_processresponse to antibiotic
C0005524molecular_functionATP binding
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0046677biological_processresponse to antibiotic
D0005524molecular_functionATP binding
D0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
D0046677biological_processresponse to antibiotic
E0005524molecular_functionATP binding
E0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
E0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE KAN A 301
ChainResidue
ASER36
APHE271
AHOH430
BHIS3
AASP165
APHE166
AASP167
AASP198
AASN234
AGLU238
AASP268
AGLU269

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0TO A 302
ChainResidue
AILE40
APHE53
ALYS55
AGLU68
ALEU72
ATHR98
AALA100
AILE101
AGLY103
ATHR105
AASP202
AILE215

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 303
ChainResidue
ATHR76
AMET79
AHOH417
AHOH433
AHOH434

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE KAN B 301
ChainResidue
BASP165
BPHE166
BASP167
BASP198
BASN234
BCYS235
BGLU238
BASP268
BGLU269
BPHE271
BHOH405
BHOH409
EGLY252

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 302
ChainResidue
BTHR76
BMET79

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE KAN C 301
ChainResidue
AGLY252
CASP165
CASP167
CASP198
CASN234
CCYS235
CGLU238
CASP268
CGLU269
CPHE271
CHOH418
CHOH437

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 0TO C 302
ChainResidue
CPHE53
CLYS55
CGLU68
CALA100
CILE101
CGLY103
CTHR105
CILE215

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 303
ChainResidue
CMET79
CPRO80

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE KAN D 301
ChainResidue
DGLN35
DASP165
DASP167
DASP198
DARG219
DASN234
DCYS235
DGLU238
DASP268
DGLU269
DPHE271
DHOH403
DHOH425

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 0TO D 302
ChainResidue
DILE40
DPHE53
DLYS55
DGLU68
DPRO82
DALA100
DILE101
DGLY103
DTHR105
DILE205
DILE215

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KAN E 301
ChainResidue
EGLU269
EPHE271
EGLN35
EASP165
EASP167
EASP198
EARG219
EASN234
ECYS235
EGLU238
EASP268

site_idBC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 0TO E 302
ChainResidue
EILE40
EPHE53
EGLU68
ELEU72
ETHR98
EALA100
EILE101
EGLY103
EILE215
EHOH428

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VTHgDFSLDNLIF
ChainResidueDetails
AVAL194-PHE206

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PDB entries from 2024-07-24

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