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1YPN

REDUCED FORM HYDROXYMETHYLBILANE SYNTHASE (K59Q MUTANT) CRYSTAL STRUCTURE AFTER 2 HOURS IN A FLOW CELL DETERMINED BY TIME-RESOLVED LAUE DIFFRACTION

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 Residues17
DetailsBINDING SITE FOR RESIDUE DPM A 314
ChainResidue
ASER81
AARG155
ALEU169
AALA170
ACYS242
AHOH336
AHOH349
AHOH376
AHOH392
ALYS83
AASP84
ATHR127
ASER128
ASER129
AARG131
AARG132
ALEU148

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_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

218853

PDB entries from 2024-04-24

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