Structure of PDB 4tn3 Chain A

Receptor sequence
>4tn3A (length=359) Species: 9544,10665 [Search protein sequence]
VDHCARHGEKLLLFCQEDSKVICWLCKDSQEHRGHHTFLMEEVAQEYHVK
LQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREI
LDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQM
MDLLQGVDGIIKRIENMTLFRAPDLKGMLDMFRDAAAEESPVLLAMNIFE
MLRIDEGLRLKIYKNTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTN
GVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQ
MGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRT
GTWDAYKNL
3D structure
PDB4tn3 Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice.
ChainA
Resolution3.1989 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E314 N323
Catalytic site (residue number reindexed from 1) E206 N215
Enzyme Commision number 3.2.1.17: lysozyme.
5.2.1.8: peptidylprolyl isomerase.
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 ZN A C108 D111 H125 H128 C15 D18 H32 H35
BS02 ZN A C97 H100 C119 C4 H7 C26
Gene Ontology
Molecular Function
GO:0003796 lysozyme activity
GO:0008270 zinc ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0009253 peptidoglycan catabolic process
GO:0016998 cell wall macromolecule catabolic process
GO:0031640 killing of cells of another organism
GO:0042742 defense response to bacterium
GO:0044659 viral release from host cell by cytolysis
Cellular Component
GO:0030430 host cell cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4tn3, PDBe:4tn3, PDBj:4tn3
PDBsum4tn3
PubMed24979782
UniProtG9MAP5;
P00720|ENLYS_BPT4 Endolysin (Gene Name=E)

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