Structure of PDB 1h54 Chain B

Receptor sequence

>1h54B (length=754) Species: 1580 (Levilactobacillus brevis)

MKRIFEVQPWNVITHTFDPKDKRLQESMTSLGNGYMGMRGDFEEGYSGDS
LQGIYLGGVWYPDKTRVGWWKNGYPKYFGKVVNAVNFIKLPIEINGEPVD
LAKDKISDFTLDLDMHQGVLNRSFVVERGAVRVALNFQRFLSVAQPELSV
QKVTVKNLSDAEVDVTLKPSIDADVMNEEANYDERFWDVLATDQQADRGS
IVAKTTPNPFGTPRFTSGMEMRLVTDLKNVAITQPNEKEVTTAYTGKLAP
QASAELEKRVIVVTSRDYDTQESLTAAMHQLSDKVAQSSYEDLLNAHTAI
WAQRWEKSDVVIKGDDESQQGIRFNLFQLFSTYYGEDARLNIGPKGFTGE
KYGGATYWDTEAFAFPVYLGITDPKVTRNLLMYRYKQLDGAYINAQEQGL
KGALFPMVTFDGIECHNEWEITFEEIHRNGDIAFAIYNYTRYTGDDSYVL
HEGAKVLTEISRFWADRVHFSKRNNQYMIHGVTGADEYENNVDNNWDTNM
LAQWTLKYTLEILGKVDQDTAKQLDVSDEEKTKWQDIVDRMYLPYDKDLN
IFVQHDGFLDKDIEPVSSIPADQRPINQNWSWDKILRSPYIKQGDVLQGI
WDFIDDYTPEQKKANFDFYEPLTVHESSLSPAIHSVLAADLHYEDKAVEL
YSRTARLDLDNYNNDTTDGLHITSMTGAWIAVVQGFAGMRVRDGQLHYAP
FLPKTWTSYTFRQVFRDRLIEVSVHADGPHFKLLSGEPLTIDVAGAAAAA
AAAA

3D structure

• PDB: 1h54 Crystal Structure of Maltose Phosphorylase from Lactobacillus Brevis: Unexpected Evolutionary Relationship with Glucoamylases.
• Chain: B
• Resolution: 2.15 Å

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.

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	PO4	B	Y352 S627 S628	Y352 S627 S628

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

External links

• PDB: RCSB:1h54, PDBe:1h54, PDBj:1h54
• PDBsum: 1h54
• PubMed: 11587643
• UniProt: Q7SIE1