Structure of PDB 1b4k Chain B

Receptor sequence
>1b4kB (length=320) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
ANRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIP
SMPGVERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPE
GIAQRATRALRERFPELGIITDVALDPFTTHGQDGILDDDGYVLNDVSID
VLVRQALSHAEAGAQVVAPSDMMDGRIGAIREALESAGHTNVRIMAYSAK
YASAYYGPFRDAVGSTYQMDPANSDEALHEVAADLAEGADMVMVKPGMPY
LDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGWLAESVILESLTAFKR
AGADGILTYFAKQAAEQLRR
3D structure
PDB1b4k High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase.
ChainB
Resolution1.67 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) K200 K245
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 SHF B Y211 F214 K260 Y283 V285 S286 Y324 Y206 F209 K245 Y268 V270 S271 Y309
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:1b4k, PDBe:1b4k, PDBj:1b4k
PDBsum1b4k
PubMed10356331
UniProtQ59643|HEM2_PSEAE Delta-aminolevulinic acid dehydratase (Gene Name=hemB)

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