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5YJL

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with NADPH and GBP

Functional Information from GO Data
ChainGOidnamespacecontents
A0008883molecular_functionglutamyl-tRNA reductase activity
A0033014biological_processtetrapyrrole biosynthetic process
A0050661molecular_functionNADP binding
B0008883molecular_functionglutamyl-tRNA reductase activity
B0033014biological_processtetrapyrrole biosynthetic process
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue NAP A 601
ChainResidue
ACYS144
ASER311
AARG314
ALEU332
ASER348
ATHR349
AALA350
ASER351
AILE380
ASER381
AVAL382
AGLN214
AHOH702
AHOH731
AHOH740
AALA256
AALA286
AGLY287
ALYS288
AMET289
AASN309
AARG310

site_idAC2
Number of Residues22
Detailsbinding site for residue NAP B 601
ChainResidue
BCYS144
BALA256
BALA286
BGLY287
BLYS288
BMET289
BASN309
BARG310
BSER311
BARG314
BLEU332
BSER348
BTHR349
BALA350
BSER351
BILE380
BVAL382
BHOH718
BHOH745
BHOH747
BHOH757
BHOH772

Functional Information from PROSITE/UniProt
site_idPS00747
Number of Residues24
DetailsGLUTR Glutamyl-tRNA reductase signature. HIfeVSAGLDSlVLGEgQILAQVK
ChainResidueDetails
AHIS193-LYS216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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