Structure of PDB 2woq Chain A

Receptor sequence

>2woqA (length=328) Species: 287 (Pseudomonas aeruginosa)

ANRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIP
SMPGVERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPE
GIAQRATRALRERFPELGIITDVALDPFTTHGQDGILDDDGYVLNDVSID
VLVRQALSHAEAGAQVVAPSDMMDGRIGAIREALESAGHTNVRIMAYSAK
YASAYYGPFRDAVGSASNLGKGNKATYQMDPANSDEALHEVAADLAEGAD
MVMVKPGMPYLDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGWLAESV
ILESLTAFKRAGADGILTYFAKQAAEQL

3D structure

• PDB: 2woq Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin.
• Chain: A
• Resolution: 1.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K205 K260
• Catalytic site (residue number reindexed from 1): K200 K255
• 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	AYC	A	D131 S175 Y202 K205 Y211 F214 K260 Y283 V285 S286 Y324	D126 S170 Y197 K200 Y206 F209 K255 Y278 V280 S281 Y319	PDBbind-CN: -logKd/Ki=2.88,Ki=1.33mM
BS02	MG	A	D131 D139 D176	D126 D134 D171
BS03	MG	A	D37 D319	D32 D314

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

External links

• PDB: RCSB:2woq, PDBe:2woq, PDBj:2woq
• PDBsum: 2woq
• PubMed: 19822707
• UniProt: Q59643|HEM2_PSEAE Delta-aminolevulinic acid dehydratase (Gene Name=hemB)