Structure of PDB 8vqr Chain B

Receptor sequence
>8vqrB (length=595) Species: 9606,34880 [Search protein sequence]
STEDLVNTFLEKFNYEAEELSYQSSLASWNYNTNITEENVQNMNNAGDKW
SAFLKEQSKLAKTYPLEEIQDSTVKRQLQALQQNGSSVLSEDKSKRLNTI
LNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWR
SEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSR
GQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGD
MWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVG
LPNMTQGFWENSMLTEPSDSWKVVCHPTAWDLGRGDFRIKMCTKVTMDDF
LTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLK
SIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIP
KDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRT
LYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLA
LENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYA
3D structure
PDB8vqr Structural evolution of SARS-CoV-2 omicron in human receptor recognition
ChainB
Resolution2.565 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.-.-
3.4.17.-
3.4.17.23: angiotensin-converting enzyme 2.
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 MAN B T347 A348 H378 T328 A329 H359
BS02 FUC B F390 L391 R393 F371 L372 R374
BS03 ZN B H374 H378 E402 H355 H359 E383
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008241 peptidyl-dipeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8vqr, PDBe:8vqr, PDBj:8vqr
PDBsum8vqr
PubMed
UniProtB4XEP4;
Q9BYF1|ACE2_HUMAN Angiotensin-converting enzyme 2 (Gene Name=ACE2)

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