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5AYV

Crystal structure of archaeal ketopantoate reductase complexed with coenzyme A and 2-oxopantoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0008677molecular_function2-dehydropantoate 2-reductase activity
A0015937biological_processcoenzyme A biosynthetic process
A0015940biological_processpantothenate biosynthetic process
A0016491molecular_functionoxidoreductase activity
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0008677molecular_function2-dehydropantoate 2-reductase activity
B0015937biological_processcoenzyme A biosynthetic process
B0015940biological_processpantothenate biosynthetic process
B0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues26
Detailsbinding site for residue NAP A 401
ChainResidue
AGLY7
ALYS74
AALA81
AGLN99
AASN100
ATHR120
AASN122
AGLY123
AALA124
AGLU262
AACT404
AGLY9
AHOH506
AHOH531
AHOH545
AHOH572
AHOH597
AHOH601
AHOH635
ASER10
AILE11
AILE29
AGLY30
AARG31
AALA72
AVAL73

site_idAC2
Number of Residues6
Detailsbinding site for residue ACT A 402
ChainResidue
ATRP288
ALYS292
AARG296
AHOH501
AHOH539
BHIS206

site_idAC3
Number of Residues1
Detailsbinding site for residue ACT A 403
ChainResidue
AARG259

site_idAC4
Number of Residues2
Detailsbinding site for residue ACT A 404
ChainResidue
AARG31
ANAP401

site_idAC5
Number of Residues2
Detailsbinding site for residue ACT A 405
ChainResidue
AGLU272
BVAL169

site_idAC6
Number of Residues23
Detailsbinding site for residue COA B 401
ChainResidue
AGLY136
ALYS137
BGLY7
BALA8
BGLY9
BSER10
BGLY30
BARG31
BILE59
BVAL73
BLYS74
BCYS84
BTRP129
BARG257
BARG259
BHOH503
BHOH505
BHOH513
BHOH519
BHOH533
BHOH583
BHOH641
BHOH683

site_idAC7
Number of Residues9
Detailsbinding site for residue KPL B 402
ChainResidue
BASN100
BTHR121
BLYS180
BASN184
BASN188
BASN198
BASN247
BASN249
BSER250

site_idAC8
Number of Residues9
Detailsbinding site for residue MPD B 403
ChainResidue
BALA135
BGLY136
BLYS137
BVAL212
BLEU234
BGLU242
BARG243
BHOH571
BHOH618

site_idAC9
Number of Residues5
Detailsbinding site for residue MPD B 404
ChainResidue
BGLY47
BALA48
BALA135
BHIS232
BGLU246

site_idAD1
Number of Residues6
Detailsbinding site for residue ACT B 405
ChainResidue
AHIS206
BTRP288
BVAL289
BLYS292
BARG296
BHOH522

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A9J4
ChainResidueDetails
ALYS180
BLYS180

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26757028, ECO:0000269|PubMed:27139828
ChainResidueDetails
AGLY7
AASN100
AALA124
AGLU262
BGLY7
BASN100
BALA124
BGLU262

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:26757028
ChainResidueDetails
AALA8
BALA8
BARG31
BCYS84
BLYS180
BASN184
BASN188
BASN198
BASN247
BARG257
AARG31
ACYS84
ALYS180
AASN184
AASN188
AASN198
AASN247
AARG257

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27139828
ChainResidueDetails
ALYS74
BLYS74

223790

PDB entries from 2024-08-14

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