Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4R1U

Crystal structure of Medicago truncatula cinnamoyl-CoA reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009699biological_processphenylpropanoid biosynthetic process
A0009809biological_processlignin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016621molecular_functioncinnamoyl-CoA reductase activity
B0005737cellular_componentcytoplasm
B0009699biological_processphenylpropanoid biosynthetic process
B0009809biological_processlignin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016621molecular_functioncinnamoyl-CoA reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 401
ChainResidue
AHIS197
AVAL210
AARG248
AHOH504

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 401
ChainResidue
BHIS197
BVAL210
BARG248
BHOH567

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 402
ChainResidue
BGLN214
BALA245
BTYR279
BPHE281
BHOH535
BTHR213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q12068
ChainResidueDetails
ALYS156
BLYS156

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A059TC02
ChainResidueDetails
AGLY8
BGLY8
BARG33
BLYS39
BASP59
BTHR79
BTYR152
BLYS156
BPRO179
BSER194
AARG33
ALYS39
AASP59
ATHR79
ATYR152
ALYS156
APRO179
ASER194

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon