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

6H0P

The structure of C100A mutant of Arabidopsis thaliana UDP-apiose/UDP-xylose synthase in complex with NADH and UDP-D-glucuronic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0009226biological_processnucleotide-sugar biosynthetic process
A0010396biological_processrhamnogalacturonan II metabolic process
A0016831molecular_functioncarboxy-lyase activity
A0033320biological_processUDP-D-xylose biosynthetic process
A0033352biological_processUDP-D-apiose biosynthetic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046982molecular_functionprotein heterodimerization activity
A0048040molecular_functionUDP-glucuronate decarboxylase activity
A0051287molecular_functionNAD binding
A0071555biological_processcell wall organization
A0102765molecular_functionUDP-D-apiose synthase activity
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0009226biological_processnucleotide-sugar biosynthetic process
B0010396biological_processrhamnogalacturonan II metabolic process
B0016831molecular_functioncarboxy-lyase activity
B0033320biological_processUDP-D-xylose biosynthetic process
B0033352biological_processUDP-D-apiose biosynthetic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046982molecular_functionprotein heterodimerization activity
B0048040molecular_functionUDP-glucuronate decarboxylase activity
B0051287molecular_functionNAD binding
B0071555biological_processcell wall organization
B0102765molecular_functionUDP-D-apiose synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY24
AALA97
AALA98
AALA100
APHE137
ASER138
ATYR185
ALYS189
AARG235
AGLY27
APHE28
AILE29
AASP49
AILE75
AASN76
AILE77
ALEU96

site_idAC2
Number of Residues24
Detailsbinding site for residue UGA A 402
ChainResidue
AALA100
APRO102
ATYR105
ATHR139
AGLU141
AARG182
ATYR185
APRO212
APHE213
AASN214
AARG235
AVAL236
ACYS239
APHE240
ALYS251
AVAL253
ASER258
AARG260
AVAL298
APHE330
ATYR331
ATYR335
AASP337
AARG341

site_idAC3
Number of Residues17
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY24
BGLY27
BPHE28
BILE29
BASP49
BILE75
BASN76
BILE77
BLEU96
BALA97
BALA98
BPHE137
BSER138
BTYR185
BLYS189
BPRO212
BARG235

site_idAC4
Number of Residues23
Detailsbinding site for residue UGA B 402
ChainResidue
BPRO102
BTYR105
BTHR139
BGLU141
BARG182
BTYR185
BPRO212
BPHE213
BASN214
BARG235
BVAL236
BCYS239
BLYS251
BLEU252
BVAL253
BSER258
BARG260
BVAL298
BPHE330
BTYR331
BTYR335
BASP337
BARG341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR185
BTYR185

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP49
BARG182
BTYR185
BASN214
BARG235
BVAL236
BVAL253
BASP337
AARG182
ATYR185
AASN214
AARG235
AVAL236
AVAL253
AASP337
BASP49

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon