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5HDM

Crystal structure of Arabidopsis thaliana glutamate-1-semialdehyde-2,1-aminomutase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0009416biological_processresponse to light stimulus
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009570cellular_componentchloroplast stroma
A0009941cellular_componentchloroplast envelope
A0015995biological_processchlorophyll biosynthetic process
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033014biological_processtetrapyrrole biosynthetic process
A0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
A0042803molecular_functionprotein homodimerization activity
A0048046cellular_componentapoplast
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006779biological_processporphyrin-containing compound biosynthetic process
B0006782biological_processprotoporphyrinogen IX biosynthetic process
B0009416biological_processresponse to light stimulus
B0009507cellular_componentchloroplast
B0009536cellular_componentplastid
B0009570cellular_componentchloroplast stroma
B0009941cellular_componentchloroplast envelope
B0015995biological_processchlorophyll biosynthetic process
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033014biological_processtetrapyrrole biosynthetic process
B0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
B0042803molecular_functionprotein homodimerization activity
B0048046cellular_componentapoplast
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue PMP A 500
ChainResidue
ASER123
AMET249
ALYS274
AHOH741
AHOH815
BTHR306
BHOH742
AGLY124
ATHR125
ATYR151
AGLY153
AGLU213
AASN218
AASP246
AVAL248

site_idAC2
Number of Residues16
Detailsbinding site for residue PMP B 502
ChainResidue
ATHR306
BSER123
BGLY124
BTHR125
BTYR151
BGLY153
BGLU213
BASN218
BASP246
BMET249
BLYS274
BPLP501
BHOH636
BHOH676
BHOH710
BHOH799

site_idAC3
Number of Residues24
Detailsbinding site for Di-peptide PLP B 501 and LYS B 274
ChainResidue
ATHR306
BTRP68
BPRO70
BSER123
BGLY124
BTHR125
BTYR151
BGLU213
BASN218
BASP246
BVAL248
BMET249
BGLY273
BILE275
BILE276
BGLY277
BGLY278
BVAL282
BPMP502
BHOH676
BHOH691
BHOH710
BHOH799
BHOH883

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues37
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVmt.GF.RlAyggaqeyfgitp....DLTtlGKiigGG
ChainResidueDetails
ALEU243-GLY279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"27303897","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HDM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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