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4RF4

Crystal structure of ketoreductase from Lactobacillus kefir

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008206biological_processbile acid metabolic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0008206biological_processbile acid metabolic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AGLN252
AGLN252
AHOH401
AHOH401
AHOH415
AHOH415

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BHOH407
BHOH413
BHOH413
BGLN252
BGLN252
BHOH407

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SiegfvgdptLgaYNASKGAVrIMSkSAA
ChainResidueDetails
ASER143-ALA171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:26644568
ChainResidueDetails
ATYR156
BTYR156

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:26644568, ECO:0007744|PDB:4RF2
ChainResidueDetails
ATHR16
BASP63
BASN90
BTYR156
BLYS160
BILE191
AARG39
AASP63
AASN90
ATYR156
ALYS160
AILE191
BTHR16
BARG39

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26644568, ECO:0007744|PDB:4RF4
ChainResidueDetails
AGLN252
BGLN252

237992

PDB entries from 2025-06-25

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