Structure of PDB 1h54 Chain B Binding Site BS01

Receptor Information
>1h54 Chain B (length=754) Species: 1580 (Levilactobacillus brevis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKRIFEVQPWNVITHTFDPKDKRLQESMTSLGNGYMGMRGDFEEGYSGDS
LQGIYLGGVWYPDKTRVGWWKNGYPKYFGKVVNAVNFIKLPIEINGEPVD
LAKDKISDFTLDLDMHQGVLNRSFVVERGAVRVALNFQRFLSVAQPELSV
QKVTVKNLSDAEVDVTLKPSIDADVMNEEANYDERFWDVLATDQQADRGS
IVAKTTPNPFGTPRFTSGMEMRLVTDLKNVAITQPNEKEVTTAYTGKLAP
QASAELEKRVIVVTSRDYDTQESLTAAMHQLSDKVAQSSYEDLLNAHTAI
WAQRWEKSDVVIKGDDESQQGIRFNLFQLFSTYYGEDARLNIGPKGFTGE
KYGGATYWDTEAFAFPVYLGITDPKVTRNLLMYRYKQLDGAYINAQEQGL
KGALFPMVTFDGIECHNEWEITFEEIHRNGDIAFAIYNYTRYTGDDSYVL
HEGAKVLTEISRFWADRVHFSKRNNQYMIHGVTGADEYENNVDNNWDTNM
LAQWTLKYTLEILGKVDQDTAKQLDVSDEEKTKWQDIVDRMYLPYDKDLN
IFVQHDGFLDKDIEPVSSIPADQRPINQNWSWDKILRSPYIKQGDVLQGI
WDFIDDYTPEQKKANFDFYEPLTVHESSLSPAIHSVLAADLHYEDKAVEL
YSRTARLDLDNYNNDTTDGLHITSMTGAWIAVVQGFAGMRVRDGQLHYAP
FLPKTWTSYTFRQVFRDRLIEVSVHADGPHFKLLSGEPLTIDVAGAAAAA
AAAA
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1h54 Chain B Residue 1755 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1h54 Crystal Structure of Maltose Phosphorylase from Lactobacillus Brevis: Unexpected Evolutionary Relationship with Glucoamylases.
Resolution2.15 Å
Binding residue
(original residue number in PDB)		Y352 S627 S628
Binding residue
(residue number reindexed from 1)		Y352 S627 S628
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E487
Catalytic site (residue number reindexed from 1) E487
Enzyme Commision number 2.4.1.8: maltose phosphorylase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1h54, PDBe:1h54, PDBj:1h54
PDBsum1h54
PubMed11587643
UniProtQ7SIE1

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