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2D2X

Crystal structure of 2-deoxy-scyllo-inosose synthase

Functional Information from GO Data
ChainGOidnamespacecontents
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
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 Residues6
DetailsBINDING SITE FOR RESIDUE CO A 601
ChainResidue
AGLU183
AHIS246
AHIS262
AHOH773
AHOH774
AHOH801

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 603
ChainResidue
ATHR106
AASP42
AGLY103
ALEU105

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 604
ChainResidue
AGLU235
AGLY239
AGLU243
AHOH630
AHOH631

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO3 A 608
ChainResidue
AGLU243
ATYR244
AGLY245
AHIS246
ATHR247
AALA273
AMET335
AILE336
AHOH628

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 602
ChainResidue
BGLU183
BHIS246
BHIS262
BGOL606
BHOH788

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO3 B 609
ChainResidue
BGLU243
BTYR244
BGLY245
BHIS246
BTHR247
BALA273
BMET335
BILE336
BHOH626

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 607
ChainResidue
AGLY104
ATHR129
ALEU131
AHOH610
AHOH635

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 605
ChainResidue
BGLY104
BTHR129
BLEU131
BHOH617
BHOH649

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 606
ChainResidue
BASP135
BGLU183
BHIS246
BHIS262
BCO602
BHOH686

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 2024-07-17

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