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7AAJ

Human porphobilinogen deaminase in complex with cofactor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004418molecular_functionhydroxymethylbilane synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0006784biological_processheme A biosynthetic process
A0006785biological_processheme B biosynthetic process
A0016740molecular_functiontransferase activity
A0018160biological_processpeptidyl-pyrromethane cofactor linkage
A0033014biological_processtetrapyrrole biosynthetic process
A0048034biological_processheme O biosynthetic process
B0004418molecular_functionhydroxymethylbilane synthase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006779biological_processporphyrin-containing compound biosynthetic process
B0006782biological_processprotoporphyrinogen IX biosynthetic process
B0006783biological_processheme biosynthetic process
B0006784biological_processheme A biosynthetic process
B0006785biological_processheme B biosynthetic process
B0016740molecular_functiontransferase activity
B0018160biological_processpeptidyl-pyrromethane cofactor linkage
B0033014biological_processtetrapyrrole biosynthetic process
B0048034biological_processheme O biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00533
Number of Residues17
DetailsPORPHOBILINOGEN_DEAM Porphobilinogen deaminase cofactor-binding site. ERaFlrhLeGGCsVPVA
ChainResidueDetails
BGLU250-ALA266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
BSER2
ASER2

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER15
BSER69
BSER147
ASER15
ASER69
ASER147

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P22907
ChainResidueDetails
BLYS74
ALYS74

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: S-(dipyrrolylmethanemethyl)cysteine => ECO:0000269|PubMed:18936296
ChainResidueDetails
BCYS261
ACYS261

222415

PDB entries from 2024-07-10

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