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2GRU

Crystal structure of 2-deoxy-scyllo-inosose synthase complexed with carbaglucose-6-phosphate, NAD+ and Co2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0003856molecular_function3-dehydroquinate synthase activity
A0009073biological_processaromatic amino acid family biosynthetic process
A0016829molecular_functionlyase activity
A0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
B0003856molecular_function3-dehydroquinate synthase activity
B0009073biological_processaromatic amino acid family biosynthetic process
B0016829molecular_functionlyase activity
B0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
B0017000biological_processantibiotic biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 601
ChainResidue
AGLU183
AHIS246
AHIS262
AEXO607
AHOH695

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO3 A 605
ChainResidue
ATHR247
AALA273
AMET335
AILE336
AHOH721
AGLU243
ATYR244
AGLY245
AHIS246

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 608
ChainResidue
ALYS141
AASN151
ALYS322
AEXO607
BARG119

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 602
ChainResidue
BGLU183
BHIS246
BHIS262
BCAK609
BHOH701

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO3 B 606
ChainResidue
BGLU243
BTYR244
BGLY245
BHIS246
BTHR247
BALA273
BMET335
BILE336
BHOH716

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD A 603
ChainResidue
AASP42
AGLY44
AVAL45
APRO46
AILE49
AGLU72
ALYS75
AGLY103
AGLY104
ALEU105
AASN108
ATHR128
ATHR129
ALEU131
ASER136
ASER139
ALYS141
AASN151
AGLN176
AHOH669
AHOH696
AHOH708
AHOH728
AHOH751

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE EXO A 607
ChainResidue
AASP135
AGLU183
ALYS186
ALYS225
AGLU235
APHE242
AGLU243
AHIS246
AHIS262
ACO601
APO4608
AHOH616
AHOH695

site_idAC8
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD B 604
ChainResidue
AARG119
BASP42
BGLY44
BVAL45
BPRO46
BILE49
BGLU72
BLYS75
BGLY103
BGLY104
BLEU105
BASN108
BTHR128
BTHR129
BLEU131
BSER136
BLYS150
BASN151
BGLN176
BCAK609
BHOH673
BHOH693
BHOH697
BHOH738
BHOH745

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CAK B 609
ChainResidue
BGLU183
BLYS186
BLYS225
BGLU235
BPHE242
BHIS246
BHIS250
BHIS262
BCO602
BNAD604
BHOH635
BHOH701
AARG119
BASP135
BLYS141
BASN151

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 611
ChainResidue
ATYR52
AARG167
AILE168
AGLU171

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 610
ChainResidue
BASN278
BASN281
BMET283

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. MISDSGVPDSIV
ChainResidueDetails
AMET39-VAL50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:17879343
ChainResidueDetails
ALYS141
AGLU243
BLYS141
BGLU243

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:17879343
ChainResidueDetails
AASP42
AHIS262
BASP42
BGLU72
BGLY104
BTHR128
BSER139
BLYS150
BGLN176
BGLU183
BHIS246
AGLU72
BHIS262
AGLY104
ATHR128
ASER139
ALYS150
AGLN176
AGLU183
AHIS246

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
AHIS250

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
BHIS250

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PDB entries from 2024-10-16

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