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5ZIK

Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa

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 Residues4
Detailsbinding site for residue SO4 A 401
ChainResidue
AGLY20
AARG21
AGLY23
APRO57

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
AASP50
APHE139
AARG142
AHOH536

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
CLEU195
CARG290
CHIS294
AARG114

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 B 401
ChainResidue
BTYR269
BHIS273
BARG276

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 B 402
ChainResidue
AASP50
BVAL194
BASP197
BVAL255
BTHR256
BHIS294
BARG298

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A9J4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues27
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa bound to NADP+.","authors":["Khanppnavar B.","Datta S."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A9J4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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