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3Q1O

Crystal structure of geranyltransferase from helicobacter pylori complexed with magnesium and isoprenyl diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0004659molecular_functionprenyltransferase activity
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0004659molecular_functionprenyltransferase activity
C0008299biological_processisoprenoid biosynthetic process
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0004659molecular_functionprenyltransferase activity
D0008299biological_processisoprenoid biosynthetic process
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 400
ChainResidue
AASP92
AASP98
AHOH312
AHOH313
ADMA501

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE DMA A 500
ChainResidue
AARG104
ATHR187
APHE224
AGLN225
AASP228
AHOH306
AHOH308
AHOH330
AHOH352
AHOH353
AHOH354
ADMA501
AGLY46
ALYS47
AARG50
AHIS85

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DMA A 501
ChainResidue
ASER88
AASP92
AASP98
AARG103
AGLN163
ALYS186
AGLN225
AASP228
ALYS242
AHOH313
AHOH314
AHOH319
AHOH320
AHOH356
AHOH382
AMG400
ADMA500

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AGLU139
ASER140

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AASN11
AARG15

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
ASER18
ALYS21
AASN22

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 400
ChainResidue
BASP92
BASP98
BHOH314
BHOH343
BDMA501

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE DMA B 500
ChainResidue
BGLY46
BLYS47
BARG50
BHIS85
BARG104
BTHR187
BPHE224
BGLN225
BASP228
BHOH308
BHOH309
BHOH334
BHOH335
BHOH336
BDMA501

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DMA B 501
ChainResidue
BSER88
BLEU89
BASP92
BASP98
BARG103
BGLN163
BLYS186
BASP228
BLYS242
BHIS245
BHOH314
BHOH316
BHOH333
BHOH337
BHOH359
BMG400
BDMA500

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BGLN267
BLYS270
BPHE299
BLYS300

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 400
ChainResidue
CASP92
CASP98
CARG103
CHOH323
CHOH325
CDMA501

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
CASP228
CHOH322
CHOH345
CDMA501

site_idBC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE DMA C 500
ChainResidue
CHIS85
CARG104
CTHR187
CPHE224
CGLN225
CASP228
CHOH311
CHOH313
CHOH317
CHOH328
CHOH350
CHOH352
CDMA501
CGLY46
CLYS47
CARG50

site_idBC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DMA C 501
ChainResidue
CSER88
CASP92
CASP98
CARG103
CGLN163
CLYS186
CASP228
CLYS242
CHOH322
CHOH323
CHOH324
CHOH325
CHOH326
CHOH327
CHOH345
CMG400
CMG401
CDMA500

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 302
ChainResidue
CALA60
CTYR284
CPRO285
CLEU286
CLEU287

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 303
ChainResidue
CASN11
CARG15

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 304
ChainResidue
CSER18
CLYS21
CASN22

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 400
ChainResidue
DASP92
DASP98
DARG103
DHOH311
DDMA501

site_idCC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DMA D 500
ChainResidue
DGLY46
DLYS47
DARG50
DHIS85
DARG104
DTHR187
DPHE224
DGLN225
DASP228
DHOH316
DHOH317
DDMA501

site_idCC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DMA D 501
ChainResidue
DSER88
DASP92
DASP98
DARG103
DLYS186
DLYS242
DHOH310
DHOH312
DHOH313
DHOH319
DHOH320
DMG400
DDMA500

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGlcFQVlDDIiD
ChainResidueDetails
AMET220-ASP232

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PDB entries from 2024-06-12

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