Structure of PDB 4hp5 Chain A

Receptor sequence

>4hp5A (length=559) Species: 55212 (Erwinia rhapontici)

NALPTWWKQAVFYQVYPRSFKDTNGDGIGDLNGIIENLDYLKKLGIDAIW
INPHYDSPNTDNGYDIRDYRKIMKEYGTMEDFDRLISEMKKRNMRLMIDI
VINHTSDQHAWFVQSKSGKNNPYRDYYFWRDGKDGHAPNNYPSFFGGSAW
EKDDKSGQYYLHYFAKQQPDLNWDNPKVRQDLYDMLRFWLDKGVSGLRFD
TVATYSKIPNFPDLSQQQLKNFAEEYTKGPKIHDYVNEMNREVLSHYDIA
TAGAIFGVPLDKSIKFFDRRRNELNIAFTFDLIRLDRDADERWRRKDWTL
SQFRKIVDKVDQTAGEYGWNAFFLDNHDNPRAVSHFGDDRPQWREHAAKA
LATLTLTQRATPFIYQGSELGMTNYPFKKIDDFDDVEVKGFWQDYVETGK
VKAEEFLQNVRQTSRDNSRTPFQWDASKNAGFTSGTPWLKINPNYKEINS
ADQINNPNSVFNYYRKLINIRHDIPALTYGSYIDLDPDNNSVYAYTRTLG
AEKYLVVINFKEEVMHYTLPGDLSINKVITENNSHTIVNKNDRQLRLEPW
QSGIYKLNP

3D structure

• PDB: 4hp5 The crystal structure of isomaltulose synthase mutant E295A from Erwinia rhapontici NX5 in complex with D-glucose
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D140 R239 D241 A295 H368 D369
• Catalytic site (residue number reindexed from 1): D99 R198 D200 A254 H327 D328
• Enzyme Commision number: 5.4.99.11: isomaltulose 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	CA	A	D63 N65 D67 I69 D71	D22 N24 D26 I28 D30
BS02	GLC	A	D102 Y105 H145 R239 D241 H368 D369 R456	D61 Y64 H104 R198 D200 H327 D328 R415

Gene Ontology

Molecular Function

• GO:0004556 alpha-amylase activity
• GO:0016853 isomerase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0009313 oligosaccharide catabolic process

External links

• PDB: RCSB:4hp5, PDBe:4hp5, PDBj:4hp5
• PDBsum: 4hp5
• UniProt: D9MPF2