Structure of PDB 1gzg Chain A

Receptor sequence
>1gzgA (length=329) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
NRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIPS
MPGVERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPEG
IAQRATRALRERFPELGIITDVALDPFTTHGQNGILDDDGYVLNDVSIDV
LVRQALSHAEAGAQVVAPSDMMDGRIGAIREALESAGHTNVRVMAYSAKY
ASAYYGPFRDAVGSASNLGKGNKATYQMDPANSDEALHEVAADLAEGADM
VMVKPGMPYLDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGWLAESVI
LESLTAFKRAGADGILTYFAKQAAEQLRR
3D structure
PDB1gzg Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism.
ChainA
Resolution1.66 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K205 K260
Catalytic site (residue number reindexed from 1) K199 K254
Enzyme Commision number 4.2.1.24: porphobilinogen synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 LAF A D131 N139 S175 K205 R215 K229 K260 D125 N133 S169 K199 R209 K223 K254
BS02 LAF A F86 S175 Y211 F214 K260 Y283 V285 S286 Y324 F80 S169 Y205 F208 K254 Y277 V279 S280 Y318
Gene Ontology
Molecular Function
GO:0004655 porphobilinogen synthase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006779 porphyrin-containing compound biosynthetic process
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0006783 heme biosynthetic process
GO:0033014 tetrapyrrole biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1gzg, PDBe:1gzg, PDBj:1gzg
PDBsum1gzg
PubMed12079382
UniProtQ59643|HEM2_PSEAE Delta-aminolevulinic acid dehydratase (Gene Name=hemB)

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