Structure of PDB 3n33 Chain C

Receptor sequence
>3n33C (length=367) Species: 364098 (Sphingosinicella xenopeptidilytica) [Search protein sequence]
GPRARDLGVPFEGTPGALNAITDVAGVEVGHTTVISGDGAMVIGKGPYRT
GVTIIHPLGKTSLDGVAAGRAVINGTGEWTGMHLVDEVGQFLGPIALTGT
GNVGLVHQSMMDWSVGKVPEEALFSRLLPVVAETLDNRLNDVFGHGLTRD
HVFAALDGAKGGPVAEGNVGGGTGMIAYTFKGGIGTSSRVVSAGDTRYTV
GVLVQANHGDRNDLRIAGVQIGKEIKGAWPEVNGIVAAGPDAGKPSLLIV
IATDAPLMPHQLERMARRAALGVGRNGSTAGALSGEFALAFSTSHVIPLG
GKPRLPAIINDTDSETMNALFRGVVQATEEALVNQLVASETMTGANNAKV
YGIPHDQLARIMKARFP
3D structure
PDB3n33 Autoproteolytic and catalytic mechanisms for the beta-aminopeptidase BapA--a member of the Ntn hydrolase family.
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L135 N207 S250 S288 G289
Catalytic site (residue number reindexed from 1) L135 N207 S246 S284 G285
Enzyme Commision number 3.4.11.25: beta-peptidyl aminopeptidase.
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 AES C T76 E133 S250 T76 E133 S246
BS02 AES C E120 F124 E120 F124
BS03 AES C F124 L128 F124 L128
BS04 AES C M41 N137 V142 F143 M41 N137 V142 F143
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0042802 identical protein binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3n33, PDBe:3n33, PDBj:3n33
PDBsum3n33
PubMed22980995
UniProtQ52VH2|BAPA_SPHXN Beta-peptidyl aminopeptidase BapA (Gene Name=bapA)

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