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6X1B

Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2 in the Complex with the Product Nucleotide GpU.

Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PO4 A 401
ChainResidue
AHIS235
AGLY248
AHIS250
ALYS290
ATHR341
AHOH560
AHOH567
DG401
DU402

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO B 501
ChainResidue
ALYS320
ATHR322
AGLU327
BVAL149
BLYS150
BGLY151
BLEU152
BHOH745

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO B 502
ChainResidue
BTHR113
BGLU114
BHOH678

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 503
ChainResidue
BSER244
BGLN245
BSER289
BHOH610
BHOH615

site_idAC5
Number of Residues9
Detailsbinding site for residue PO4 B 504
ChainResidue
BHIS235
BGLY248
BHIS250
BLYS290
BTHR341
BTYR343
FG401
FU402
FHOH502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093
ChainResidueDetails
AHIS235
BHIS235

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093
ChainResidueDetails
AHIS250
BHIS250

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: For uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779
ChainResidueDetails
ALYS290
BLYS290

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093
ChainResidueDetails
ALYS290
BLYS290

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:33564093
ChainResidueDetails
ATHR341
BTHR341

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093
ChainResidueDetails
ALYS290
BLYS290

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Uracil recognition site => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093
ChainResidueDetails
ASER294
BSER294

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
ChainResidueDetails
AGLN347
BGLN347

223790

PDB entries from 2024-08-14

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