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1H7P

SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH 4-KETO-5-AMINO-HEXANOIC (KAH) AT 1.64 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004655molecular_functionporphobilinogen synthase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006779biological_processporphyrin-containing compound biosynthetic process
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
AHOH2349

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KAH A1341
ChainResidue
ALYS263
ATYR287
AVAL289
ASER290
ATYR329
AHOH2203
APHE89
AASP131
ATYR207
ALYS210
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
DetailsActive site: {"description":"Schiff-base intermediate with substrate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

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PDB entries from 2025-08-27

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