8VKN

Cryo-EM structure of SARS-CoV-2 XBB.1.5 spike protein in complex with mouse ACE2 (focused refinement of RBD and mouse ACE2)

Functional Information from GO Data

Chain	GOid	namespace	contents
D	0006508	biological_process	proteolysis
D	0008237	molecular_function	metallopeptidase activity
D	0008241	molecular_function	peptidyl-dipeptidase activity
D	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ

Chain	Residue	Details
D	THR371-GLN380

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site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. ATSTdyNsRLWAWEG

Chain	Residue	Details
D	ALA153-GLY167

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	GLU375
A	THR346

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	HIS505

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	ARG169
D	HIS374
D	HIS378
D	GLU402
D	TRP477
D	LYS481

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1

Chain	Residue	Details
D	ARG273
D	HIS345
D	TYR515

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site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
D	ASN53
D	ASN536
D	ASN546

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