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3HAV

Structure of the streptomycin-ATP-APH(2")-IIa ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0005524molecular_functionATP binding
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0005524molecular_functionATP binding
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 401
ChainResidue
ALEU24
AILE209
AASP210
AHOH309
AHOH320
AHOH342
AHOH373
AMG402
ASER25
ASER30
ATHR32
ALYS42
AMET85
ALYS86
ATYR87
AILE88

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AASP210
AHOH321
AHOH352
AATP401

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SRY A 403
ChainResidue
AASP192
ASER194
AASP213
ACYS225
AASP232
AASP262
ATRP265
ATYR272
AHOH344

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 401
ChainResidue
BLEU24
BSER25
BSER30
BTHR32
BLYS42
BMET85
BLYS86
BTYR87
BILE88
BILE209
BASP210
BHOH316
BHOH333
BHOH346
BHOH348
BHOH357
BMG402

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BASP210
BATP401

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SRY B 403
ChainResidue
BASN191
BASP192
BASP213
BCYS225
BASN261
BASP262
BTRP265
BTYR272
BHOH348

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP C 401
ChainResidue
CLEU24
CSER25
CSER30
CTHR32
CLYS42
CMET85
CLYS86
CTYR87
CILE88
CILE209
CASP210
CHOH300
CHOH307
CHOH319
CHOH322
CHOH331
CHOH339
CHOH356
CMG402

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 402
ChainResidue
CASP210
CATP401

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SRY C 403
ChainResidue
CASN191
CASP192
CSER194
CASP213
CCYS225
CSER230
CASP232
CASN261
CASP262
CTRP265
CTYR272
CHOH341

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHnDFSANNMIF
ChainResidueDetails
ALEU188-PHE200

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
AASP192
ALYS42

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
BASP192
BLYS42

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
CASP192
CLYS42

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PDB entries from 2024-07-24

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