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6K1R

Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa in complex with NAD+ and ketopantoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008677molecular_function2-dehydropantoate 2-reductase activity
A0015940biological_processpantothenate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050661molecular_functionNADP binding
B0005737cellular_componentcytoplasm
B0008677molecular_function2-dehydropantoate 2-reductase activity
B0015940biological_processpantothenate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0050661molecular_functionNADP binding
C0005737cellular_componentcytoplasm
C0008677molecular_function2-dehydropantoate 2-reductase activity
C0015940biological_processpantothenate biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 401
ChainResidue
ATHR126
AHIS144
ATRP146
AHOH526
BARG296

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 402
ChainResidue
AARG142
AGLU49
APHE139
AALA140
AGLY141

site_idAC3
Number of Residues6
Detailsbinding site for residue KPL A 403
ChainResidue
AASN186
AILE189
AASN190
AASN200
ASER249
ASER250

site_idAC4
Number of Residues20
Detailsbinding site for residue NAD A 404
ChainResidue
AGLY7
AALA8
AGLY9
ASER10
ALEU11
AARG31
AALA75
ACYS76
ALYS77
AASP80
AALA84
ALEU101
AASN103
ASER125
AGLU127
AGLY128
AALA129
AARG131
AGLU262
AHOH528

site_idAC5
Number of Residues5
Detailsbinding site for residue KPL B 401
ChainResidue
BASN190
BASN200
BVAL240
BSER249
BSER250

site_idAC6
Number of Residues22
Detailsbinding site for residue NAD B 402
ChainResidue
BLEU6
BGLY7
BALA8
BGLY9
BSER10
BLEU11
BARG31
BALA75
BCYS76
BLYS77
BASP80
BLEU101
BGLN102
BASN103
BSER125
BGLU127
BGLY128
BALA129
BARG131
BGLU262
BHOH504
BHOH521

site_idAC7
Number of Residues6
Detailsbinding site for residue KPL C 401
ChainResidue
CLEU185
CASN190
CASN200
CSER249
CSER250
CHOH526

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A9J4
ChainResidueDetails
ALYS182
BLYS182
CLYS182

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|Ref.3
ChainResidueDetails
AARG131
AGLU262
BGLY7
BARG35
BALA129
BARG131
BGLU262
CGLY7
CARG35
CALA129
CARG131
CGLU262
AGLY7
AARG35
AALA129

site_idSWS_FT_FI3
Number of Residues15
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A9J4
ChainResidueDetails
BSER250
CASN103
CASN186
CASN190
CASN200
CSER250
AASN103
AASN186
AASN190
AASN200
ASER250
BASN103
BASN186
BASN190
BASN200

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PDB entries from 2024-05-15

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