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8GRY

Cryo-EM structure of SARS-CoV-2 Omicron BA.2 RBD in complex with rat ACE2 (local refinement)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ATHR371-GLN380

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ATSTdyNrRLWAWEG
ChainResidueDetails
AALA153-GLY167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BASN343

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AHIS505

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AARG169
AHIS374
AHIS378
AGLU402
ATRP477
ALYS481

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1
ChainResidueDetails
AARG273
AHIS345
ATYR515

site_idSWS_FT_FI5
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN53
AASN82
AASN90
AASN299
AASN432
AASN546
AASN601

221051

PDB entries from 2024-06-12

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