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6H0N

The structure of wild-type Arabidopsis thaliana UDP-apiose/UDP-xylose synthase in complex with NAD+ and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0009226biological_processnucleotide-sugar biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0048040molecular_functionUDP-glucuronate decarboxylase activity
A0051287molecular_functionNAD binding
A0071555biological_processcell wall organization
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0009226biological_processnucleotide-sugar biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0048040molecular_functionUDP-glucuronate decarboxylase activity
B0051287molecular_functionNAD binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY24
AILE77
ALEU96
AALA97
AALA98
ACYS100
APHE137
ASER138
ATHR139
ATYR185
ALYS189
AGLY26
APRO212
AASN214
ATRP215
AARG235
APO4403
AGLY27
APHE28
AILE29
AASP49
AVAL50
AILE75
AASN76

site_idAC2
Number of Residues18
Detailsbinding site for residue UDP A 402
ChainResidue
APRO102
AGLU141
AARG182
AASN214
AARG235
AVAL236
ACYS239
ALYS251
ALEU252
AVAL253
AARG260
AVAL298
APHE330
ATYR331
ATYR335
AASP337
AARG341
APO4403

site_idAC3
Number of Residues8
Detailsbinding site for residue PO4 A 403
ChainResidue
ACYS100
ATYR105
ATHR139
AGLU141
ATYR185
AARG235
ANAD401
AUDP402

site_idAC4
Number of Residues22
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY24
BGLY26
BGLY27
BPHE28
BILE29
BASP49
BILE75
BASN76
BILE77
BLEU96
BALA97
BALA98
BCYS100
BPHE137
BSER138
BTHR139
BTYR185
BLYS189
BPRO212
BTRP215
BARG235
BPO4403

site_idAC5
Number of Residues18
Detailsbinding site for residue UDP B 402
ChainResidue
BPRO102
BGLU141
BARG182
BASN214
BARG235
BVAL236
BCYS239
BLYS251
BLEU252
BVAL253
BARG260
BVAL298
BPHE330
BTYR331
BTYR335
BASP337
BARG341
BPO4403

site_idAC6
Number of Residues8
Detailsbinding site for residue PO4 B 403
ChainResidue
BCYS100
BTYR105
BTHR139
BGLU141
BTYR185
BARG235
BNAD401
BUDP402

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

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PDB entries from 2024-07-24

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