Structure of PDB 1t1e Chain A

Receptor sequence
>1t1eA (length=534) Species: 198803 (Bacillus sp. MN-32) [Search protein sequence]
EKREVLAGHARRQAPQAVDKGPVTGDQRISVTVVLRRQRGDELEAHVERQ
AALAPHARVHLEREAFAASHGASLDDFAEIRKFAEAHGLTLDRAHVAAGT
AVLSGPVDAVNQAFGVELRHFDHPDGSYRSYVGDVRVPASIAPLIEAVLG
LDTRPVARPHFRLRRRAEGEFEARSQSAAPTAYTPLDVAQAYQFPEGLDG
QGQCIAIIELGGGYDETSLAQYFASLGVSAPQVVSVSVDGATNQPTGDPN
GPDGEVELDIEVAGALAPGAKIAVYFAPNTDAGFLNAITTAVHDPTHKPS
IVSISWGGPEDSWAPASIAAMNRAFLDAAALGVTVLAAAGDSGSTDGEQD
GLYHVDFPAASPYVLACGGTRLVASAGRIERETVWNDGPDGGSTGGGVSR
IFPLPSWQERANVPPSANPGAGSGRGVPDVAGNADPATGYEVVIDGETTV
IGGTAAVAPLFAALVARINQKLGKPVGYLNPTLYQLPPEVFHDITEGNND
IANRARIYQAGPGWDPCTGLGSPIGIRLLQALLP
3D structure
PDB1t1e 1.2 a crystal structure of the serine carboxyl proteinase pro-kumamolisin: structure of an intact pro-subtilase
ChainA
Resolution1.18 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E267 D271 D353 A467
Catalytic site (residue number reindexed from 1) E255 D259 D341 A455
Enzyme Commision number ?
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 D505 I506 G523 G525 D527 D493 I494 G511 G513 D515
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0008240 tripeptidyl-peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1t1e, PDBe:1t1e, PDBj:1t1e
PDBsum1t1e
PubMed15242607
UniProtQ8RR56

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