Structure of PDB 6fw2 Chain A

Receptor sequence
>6fw2A (length=444) Species: 9606,10665 [Search protein sequence]
MQQVGTVAQLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVINQEG
NMVTARQEPRLVLISLTCDGDTLTLSAMNIFEMLRIDEGLRLKIYKDTEG
YYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDA
AVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQ
KRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYTKDLLLPIKTPT
TNAVHKCRVHGLEIEGRDCGEAAAQWITSFLKSQPYRLVHFEPHMRPRRP
HQIADLFRPKDQIAYSDTSPFLILSEASLADLNSRLEKKVKATNFRPNIV
ISGCDVYAEDSWDELLIGDVELKRVMACSRCILTTVDPDTGVMSRKEPLE
TLKSYRQCDPSERKLYGKSPLFGQYFVLENPGTIKVGDPVYLLG
3D structure
PDB6fw2 Crystal structure of human mARC1 reveals its exceptional position among eukaryotic molybdenum enzymes.
ChainA
Resolution1.78 Å
3D
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
Enzyme Commision number 1.7.-.-
3.2.1.17: lysozyme.
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 EFK A R272 C273 R380 C381
BS02 MOO A R1014 L1015 K1016 R91 L92 K93
BS03 MOO A F1114 N1116 S1117 N1132 F191 N193 S194 N209
BS04 MOO A T1142 N1144 R1145 T219 N221 R222
Gene Ontology
Molecular Function
GO:0003796 lysozyme activity
GO:0003824 catalytic activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030151 molybdenum ion binding
GO:0030170 pyridoxal phosphate binding
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6fw2, PDBe:6fw2, PDBj:6fw2
PDBsum6fw2
PubMed30397129
UniProtP00720|ENLYS_BPT4 Endolysin (Gene Name=E);
Q5VT66

[Back to BioLiP]