Structure of PDB 1q5p Chain A

Receptor sequence
>1q5pA (length=269) Species: 1467 (Lederbergia lenta) [Search protein sequence]
AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFV
PGEPSTQDGNGHGTHVAGTIAALDNSIGVLGVAPSAELYAVKVLGASGSG
AISSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAA
SGNEGAGSIDYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQ
STYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATS
LGSTNLYGSGLVNAEAATR
3D structure
PDB1q5p Do enzymes change the nature of transition states? Mapping the transition state for general acid-base catalysis of a serine protease
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 H62 N153 S215
Catalytic site (residue number reindexed from 1) D32 H62 N153 S215
Enzyme Commision number 3.4.21.62: subtilisin.
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 Q2 D40 L73 N75 I77 V79 Q2 D40 L73 N75 I77 V79
BS02 CA A A163 R164 Y165 A168 G189 A163 R164 Y165 A168 G189
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0030435 sporulation resulting in formation of a cellular spore
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q5p, PDBe:1q5p, PDBj:1q5p
PDBsum1q5p
PubMed12962477
UniProtP29600|SUBS_LEDLE Subtilisin Savinase

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