Structure of PDB 3n33 Chain B

Receptor sequence
>3n33B (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.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B F124 L128 F124 L128
BS02 AES B N137 V142 N137 V142
BS03 AES B T76 E133 S250 T76 E133 S246
BS04 AES B E120 L123 F124 L127 E120 L123 F124 L127
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0042802 identical protein binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0042597 periplasmic space

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

[Back to BioLiP]