Structure of PDB 2aph Chain B

Receptor sequence
>2aphB (length=165) Species: 9606 (Homo sapiens) [Search protein sequence]
VCPNIIKRSAWEARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRN
IQSFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIA
FIGYFVEKPPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPG
QALYNIISTWPHFKH
3D structure
PDB2aph Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y242
Catalytic site (residue number reindexed from 1) Y66
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 peptide B D318 H341 D142 H165
BS02 peptide B T209 H231 N236 F237 Y242 S263 H264 Y266 G267 N269 V320 S324 T33 H55 N60 F61 Y66 S87 H88 Y90 G91 N93 V144 S148
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity
GO:0042834 peptidoglycan binding
Biological Process
GO:0009253 peptidoglycan catabolic process
GO:0045087 innate immune response

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2aph, PDBe:2aph, PDBj:2aph
PDBsum2aph
PubMed16641493
UniProtQ96LB9|PGRP3_HUMAN Peptidoglycan recognition protein 3 (Gene Name=PGLYRP3)

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