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3ECR

Structure of human porphobilinogen deaminase

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 PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE DPM A 365
ChainResidue
ASER99
ALEU191
AALA192
AGLN220
AGLY221
ACYS264
AHOH366
ALYS101
AASP102
ATHR148
ASER149
ASER150
AARG152
AARG153
AARG176

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DPM B 365
ChainResidue
BILE74
BSER99
BLYS101
BASP102
BSER149
BSER150
BARG152
BARG153
BARG176
BLEU191
BALA192
BGLN220
BGLY221
BCYS264
BHOH370
BHOH371
BHOH385
BHOH401
BHOH410

Functional Information from PROSITE/UniProt
site_idPS00533
Number of Residues17
DetailsPORPHOBILINOGEN_DEAM Porphobilinogen deaminase cofactor-binding site. ERaFlrhLeGGCsVPVA
ChainResidueDetails
AGLU253-ALA269

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
ASER5
BSER5

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER18
ASER72
ASER150
BSER18
BSER72
BSER150

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P22907
ChainResidueDetails
ALYS77
BLYS77

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: S-(dipyrrolylmethanemethyl)cysteine => ECO:0000269|PubMed:18936296
ChainResidueDetails
ACYS264
BCYS264

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PDB entries from 2024-04-17

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