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3CSD

Actinorhodin Polyketide Ketoreductase Mutant P94L bound to NADPH and the Inhibitor Emodin

Functional Information from GO Data
ChainGOidnamespacecontents
A0008202biological_processsteroid metabolic process
A0016491molecular_functionoxidoreductase activity
A0017000biological_processantibiotic biosynthetic process
B0008202biological_processsteroid metabolic process
B0016491molecular_functionoxidoreductase activity
B0017000biological_processantibiotic biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NDP B 301
ChainResidue
BGLY13
BVAL64
BASN90
BALA143
BTYR157
BLYS161
BPRO187
BGLY188
BVAL190
BTHR192
BPRO193
BTHR15
BMET194
BEMO303
BHOH328
BHOH362
BSER16
BGLY17
BILE18
BARG38
BGLY39
BCYS62
BASP63

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EMO B 302
ChainResidue
BSER144
BTHR145
BGLY146
BGLN149
BVAL151
BTYR157
BVAL198
BLEU258
BEMO303

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EMO B 303
ChainResidue
BSER144
BTYR157
BGLY188
BPHE189
BMET194
BVAL198
BILE217
BLEU258
BNDP301
BEMO302

site_idAC4
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NDP A 301
ChainResidue
AGLY13
ATHR15
ASER16
AGLY17
AILE18
AALA37
AARG38
AGLY39
ACYS62
AASP63
AVAL64
AASN90
AALA91
AGLY92
AILE142
AALA143
ATYR157
ALYS161
APRO187
AGLY188
AVAL190
ATHR192
APRO193
AMET194
AEMO302
AHOH305
AHOH306
AHOH362
AHOH374
BARG51
BHOH348

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EMO A 302
ChainResidue
ASER144
ATHR145
ATYR157
AGLY188
APHE189
AVAL198
AILE217
ALEU258
ANDP301
AEMO303

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EMO A 303
ChainResidue
ALEU94
ASER144
ATHR145
AGLY146
AGLN149
AVAL151
ATYR157
AEMO302

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. StggkqgvvhAapYSASKHGVvGFTkALG
ChainResidueDetails
BSER144-GLY172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
BTYR157
ATYR157

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323
ChainResidueDetails
BVAL11
BASP63
BLYS161
AVAL11
AASP63
ALYS161

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BSER144
ASER144

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BASN114
BLYS161
BSER144
BTYR157

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
AASN114
ALYS161
ASER144
ATYR157

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BALA154
BLYS161

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
AALA154
ALYS161

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BLYS161
BTYR157

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS161
ATYR157

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PDB entries from 2024-07-24

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