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2GS8

Structure of mevalonate pyrophosphate decarboxylase from Streptococcus pyogenes

Functional Information from GO Data
ChainGOidnamespacecontents
A0004163molecular_functiondiphosphomevalonate decarboxylase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0008299biological_processisoprenoid biosynthetic process
A0016301molecular_functionkinase activity
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019287biological_processisopentenyl diphosphate biosynthetic process, mevalonate pathway
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 501
ChainResidue
APHE50
AGLN87
AALA88
AHOH757
AHOH911
AHOH990
AHOH1053

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
ASER10
AALA113
ALYS116
ASER145
APHE146
AHOH612
AHOH634
AHOH690
AVAL8
ATHR9

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLN120
AGLN125
APRO246
APHE247
AHOH621
AHOH651
AHOH804
AHOH968

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AGLN59
ATYR61
ASER76
AALA77
AASP80
AHOH723
AHOH857

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AILE14
ALEU104
AMSE173
ALYS282
AHOH639
AHOH645
AHOH900

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AGLN87
AMSE258
AGLU259
ALYS262
AEDO507
AHOH684
AHOH1069

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AGLN87
ALYS241
ATYR255
AEDO506
AEDO508
AHOH657
AHOH708

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
AGLN87
APHE122
ATYR255
AEDO507
AHOH847

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
ATYR19
ASER141
ASER185
AHOH638
AHOH672
AHOH785

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 601
ChainResidue
ATHR9
ATHR45
AASP166

Functional Information from PROSITE/UniProt
site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. MPtAaGLSSSSS
ChainResidueDetails
AMSE98-SER109

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fwk
ChainResidueDetails
APRO182

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PDB entries from 2024-07-17

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