Structure of PDB 3hpf Chain B

Receptor sequence

>3hpfB (length=387) Species: 221109 (Oceanobacillus iheyensis HTE831)

MKITDLELHAVGIPRHTGFVNKHVIVKIHTDEGLTGIGEMSDFSHLPLYS
VDLHDLKQGLLSILLGQNPFDLMKINKELTDNFPETMYYFEKGSFIRNGI
DNALHDLCAKYLDISVSDFLGGRVKEKIKVCYPIFRHRFSEEVESNLDVV
RQKLEQGFDVFRLYVGKNLDADEEFLSRVKEEFGSRVRIKSYDFSHLLNW
KDAHRAIKRLTKYDLGLEMIESPAPRNDFDGLYQLRLKTDYPISEHVWSF
KQQQEMIKKDAIDIFNISPVFIGGLTSAKKAAYAAEVASKDVVLGTTQEL
SVGTAAMAHLGCSLTNINHTSDPTGPELYVGDVVKNRVTYKDGYLYAPDR
SVKGLGIELDESLLAKYQVPDLSWDNVTVHQLQDRTA

3D structure

• PDB: 3hpf Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis .
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D42 H45 F90 P133 R162 Y164 Y192 D193 F194 M219 E221 S244 E245 H246 S268 G295 T296 T297 S321 D322
• Catalytic site (residue number reindexed from 1): D42 H45 F90 P133 R162 Y164 Y192 D193 F194 M219 E221 S244 E245 H246 S268 G295 T296 T297 S321 D322
• Enzyme Commision number: 4.2.1.158: galactarate dehydratase (D-threo-forming).

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	GAE	B	R15 H45 Y89 R162 Y164 D193 H246 T296 T297 Q298 R385	R15 H45 Y89 R162 Y164 D193 H246 T296 T297 Q298 R385
BS02	MG	B	D193 E221 H246	D193 E221 H246
BS03	MG	B	D42 H45 T297	D42 H45 T297

Gene Ontology

Molecular Function

• GO:0016829 lyase activity
• GO:0046872 metal ion binding

External links

• PDB: RCSB:3hpf, PDBe:3hpf, PDBj:3hpf
• PDBsum: 3hpf
• PubMed: 19883118
• UniProt: Q8EMJ9|GALRD_OCEIH Galactarate dehydratase (D-threo-forming) (Gene Name=OB2843)