Structure of PDB 4hph Chain A

Receptor sequence
>4hphA (length=559) Species: 55212 (Erwinia rhapontici) [Search protein sequence]
NALPTWWKQAVFYQVYPRSFKDTNGDGIGDLNGIIENLDYLKKLGIDAIW
INPHYDSPNTDNGYDIRDYRKIMKEYGTMEDFDRLISEMKKRNMRLMIDI
VINHTSDQHAWFVQSKSGKNNPYRDYYFWRDGKDGHAPNNYPSFFGGSAW
EKDDKSGQYYLHYFAKQQPDLNWDNPKVRQDLYDMLRFWLDKGVSGLRFD
TVATYSKIPNFPDLSQQQLKNFAEEYTKGPKIHDYVNEMNREVLSHYDIA
TAGQIFGVPLDKSIKFFDRRRNELNIAFTFDLIRLDRDADERWRRKDWTL
SQFRKIVDKVDQTAGEYGWNAFFLDNHDNPRAVSHFGDDRPQWREHAAKA
LATLTLTQRATPFIYQGSELGMTNYPFKKIDDFDDVEVKGFWQDYVETGK
VKAEEFLQNVRQTSRDNSRTPFQWDASKNAGFTSGTPWLKINPNYKEINS
ADQINNPNSVFNYYRKLINIRHDIPALTYGSYIDLDPDNNSVYAYTRTLG
AEKYLVVINFKEEVMHYTLPGDLSINKVITENNSHTIVNKNDRQLRLEPW
QSGIYKLNP
3D structure
PDB4hph The Structural Basis of Erwinia rhapontici Isomaltulose Synthase
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D140 R239 D241 Q295 H368 D369
Catalytic site (residue number reindexed from 1) D99 R198 D200 Q254 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 GLC A D102 Y105 H145 F205 D241 Q295 H368 D369 R456 D61 Y64 H104 F164 D200 Q254 H327 D328 R415
BS02 FRU A F205 Q295 F297 D369 E428 R456 F164 Q254 F256 D328 E387 R415
BS03 CA A D63 N65 D67 I69 D71 D22 N24 D26 I28 D30
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4hph, PDBe:4hph, PDBj:4hph
PDBsum4hph
PubMed24069347
UniProtD9MPF2

[Back to BioLiP]