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1EB3

YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004655molecular_functionporphobilinogen synthase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0033014biological_processtetrapyrrole biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1342
ChainResidue
ACYS133
ACYS135
ACYS143
AHOH2402

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE DSB A1341
ChainResidue
AARG220
AARG232
AGLN236
ALYS263
ATYR287
AVAL289
ASER290
ATYR329
AHOH2401
AHOH2402
APHE89
ASER179
ALYS210
ATYR216
APHE219

Functional Information from PROSITE/UniProt
site_idPS00169
Number of Residues13
DetailsD_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDgIIVKPStfY
ChainResidueDetails
AGLY256-TYR268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate
ChainResidueDetails
ALYS210
ALYS263

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
ACYS133
ACYS135
ACYS143
AARG220
AARG232
ASER290
ATYR329

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER254

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7o
ChainResidueDetails
ASER179
AASP131
ALYS263
ALYS210

226707

PDB entries from 2024-10-30

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