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5JCL

Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003729molecular_functionmRNA binding
A0005737cellular_componentcytoplasm
A0005782cellular_componentperoxisomal matrix
A0016491molecular_functionoxidoreductase activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
A0016656molecular_functionmonodehydroascorbate reductase (NADH) activity
A0098869biological_processcellular oxidant detoxification
B0000166molecular_functionnucleotide binding
B0003729molecular_functionmRNA binding
B0005737cellular_componentcytoplasm
B0005782cellular_componentperoxisomal matrix
B0016491molecular_functionoxidoreductase activity
B0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
B0016656molecular_functionmonodehydroascorbate reductase (NADH) activity
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue FAD A 500
ChainResidue
AGLY13
APRO49
ASER52
ALYS53
ATHR94
AGLU95
AILE96
AALA122
ATHR123
AGLY124
AARG147
AGLY14
AGLU148
ALEU268
AGLY297
AASP298
AGLU314
AHIS315
AVAL316
AALA319
ATYR349
ANDP501
AGLY15
AHOH682
AHOH738
AHOH751
AHOH752
AHOH763
AHOH781
AVAL16
AALA17
ASER39
ALYS40
AGLU41
AARG48

site_idAC2
Number of Residues26
Detailsbinding site for residue NDP A 501
ChainResidue
AGLY171
AGLY173
ATYR174
AILE175
AGLU178
APRO195
AARG202
AGLY259
AVAL260
AGLY261
AGLU314
AHIS315
ATYR349
AFAD500
AHOH684
AHOH711
AHOH716
AHOH753
AHOH763
AHOH772
AHOH775
AHOH820
AHOH823
AHOH826
AHOH857
BHOH632

site_idAC3
Number of Residues30
Detailsbinding site for residue NDP B 501
ChainResidue
BGLY171
BGLY173
BTYR174
BILE175
BGLU178
BPRO195
BVAL228
BGLY259
BVAL260
BGLY261
BGLU314
BHIS315
BTYR349
BFAD502
BHOH601
BHOH602
BHOH604
BHOH633
BHOH659
BHOH685
BHOH692
BHOH702
BHOH718
BHOH762
BHOH768
BHOH776
BHOH777
BHOH804
BHOH832
BHOH895

site_idAC4
Number of Residues33
Detailsbinding site for residue FAD B 502
ChainResidue
BARG48
BPRO49
BSER52
BLYS53
BTHR94
BILE96
BALA122
BTHR123
BGLY124
BARG147
BGLU148
BLEU268
BGLY297
BASP298
BGLU314
BHIS315
BVAL316
BALA319
BTYR349
BNDP501
BHOH637
BHOH644
BHOH648
BHOH659
BHOH749
BGLY13
BGLY14
BGLY15
BVAL16
BALA17
BSER39
BLYS40
BGLU41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:27652777, ECO:0007744|PDB:5JCI
ChainResidueDetails
AGLY14
BGLU41
BARG48
BLYS53
BILE96
BARG147
BASP298
BVAL316
AGLU41
AARG48
ALYS53
AILE96
AARG147
AASP298
AVAL316
BGLY14

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27652777, ECO:0007744|PDB:5JCK
ChainResidueDetails
AGLY172
AALA196
BGLY172
BALA196

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27652777, ECO:0007744|PDB:5JCL
ChainResidueDetails
ATYR174
BTYR349
AARG202
AGLY261
AGLU314
ATYR349
BTYR174
BARG202
BGLY261
BGLU314

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27652777, ECO:0007744|PDB:5JCN
ChainResidueDetails
AARG320
AARG351
BARG320
BARG351

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PDB entries from 2024-10-09

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