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1GTK

Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004418molecular_functionhydroxymethylbilane synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0016740molecular_functiontransferase activity
A0018160biological_processpeptidyl-pyrromethane cofactor linkage
A0033014biological_processtetrapyrrole biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE DPM A 315
ChainResidue
ALEU15
ALEU148
AARG155
ALEU169
AALA170
AGLN198
AGLY199
ACYS242
AHOH2197
AHOH2317
AHOH2318
ASER81
AHOH2319
AHOH2320
ALYS83
AASP84
ATHR127
ASER128
ASER129
AARG131
AARG132

Functional Information from PROSITE/UniProt
site_idPS00533
Number of Residues17
DetailsPORPHOBILINOGEN_DEAM Porphobilinogen deaminase cofactor-binding site. ERaMntrLeGGCqVPIG
ChainResidueDetails
AGLU231-GLY247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: S-(dipyrrolylmethanemethyl)cysteine
ChainResidueDetails
ACYS242

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 2ypn
ChainResidueDetails
ACYS242
AARG155
AASP84
AARG131
AARG149
AARG132

site_idMCSA1
Number of Residues7
DetailsM-CSA 260
ChainResidueDetails
ALYS83activator, electrostatic stabiliser, hydrogen bond donor
AASP84hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AARG131activator, electrostatic stabiliser, hydrogen bond donor
AARG132activator, electrostatic stabiliser, hydrogen bond donor
AARG149activator, electrostatic stabiliser
AARG155activator, electrostatic stabiliser
ACYS242covalently attached

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PDB entries from 2025-06-18

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