Structure of PDB 5brp Chain B

Receptor sequence
>5brpB (length=555) Species: 279010 (Bacillus licheniformis DSM 13 = ATCC 14580) [Search protein sequence]
NPWWKKAVVYQIYPKSFKDTTGNGVGDIRGIIEKLDYIKELACDVIWLTP
IYQSPQNDNGYDISDYYSIHEEYGTMADFEELLEEAHKRGIKVIMDLVVN
HTSTEHRWFKEAASGKENLYRDFYIWKDMKPNGAPPTNWESKFGGSAWEF
HAESGQYYLHLYDVTQADLNWENEAVRKKVYEMMHFWFEKGIDGFQLDVI
NVISKDQRFPDDDEGDGRRFYTDGPRVHEFLNEMNREVFSKYDSMTVGEM
SSTTIADCIRYTNPESRELDMVFNFHHLKADYPNGEKWALADFDFLKLKK
ILSEWQTEMNKGGGWNALFWCNHDQPRIVSRYGDDGKYRKKSAKMLATAI
HMLQGTPYIYQGEELGMTNPKFDDISLYRDVESLNMYRILKEAGKPEAEI
IEILKAKSRDNSRTPVQWNGEENAGFTAGTPWIPVPDNYKEINAEEALND
PDSIFYHYKKLNELRKEFDIITTGDYQLILEDDQELYAYLRNGADEKLLV
INNFYGKETEFQLPDDIDIEGYDAKVLISNDTDLPESFKRFTVKPYQSIV
YHLAK
3D structure
PDB5brp Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity
ChainB
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D101 Q201 D203 E254 H328 D329
Catalytic site (residue number reindexed from 1) D96 Q196 D198 E249 H323 D324
Enzyme Commision number 3.2.1.93: alpha,alpha-phosphotrehalase.
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 PNG B D63 N64 Y66 H106 F148 Y167 D203 E254 D58 N59 Y61 H101 F143 Y162 D198 E249
BS02 MG B D24 T26 N28 V30 D32 D19 T21 N23 V25 D27
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0008788 alpha,alpha-phosphotrehalase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005991 trehalose metabolic process
GO:0005993 trehalose catabolic process
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5brp, PDBe:5brp, PDBj:5brp
PDBsum5brp
PubMed26894535
UniProtQ65MI2

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