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6VWW

Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2.

Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 401
ChainResidue
ALEU43
APHE44
AGLU45
AGLU267
AHOH623

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 402
ChainResidue
AGLY147
AGLY126
AARG127
ATHR145
AGLU146

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
ASER262
APRO263
AASP283
AALA284
AGLN285

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AGLY77
AASP79
APRO119
AHOH518

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL A 405
ChainResidue
AGLU69
ALYS90
ATHR167
ASER198
AASN200
AHOH542
AHOH547
AHOH555

site_idAC6
Number of Residues3
Detailsbinding site for residue ACY A 406
ChainResidue
AASN200
ALEU201
ATYR279

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 401
ChainResidue
BASN75
BSER274
BTHR275
BVAL276
BHOH530

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL B 402
ChainResidue
BLYS90
BTHR167
BSER198
BARG199
BASN200
BHOH501

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL B 403
ChainResidue
BGLY77
BASP79
BPRO119
BTHR121
BHOH509

site_idAD1
Number of Residues3
Detailsbinding site for residue CL B 404
ChainResidue
ATHR322
BVAL149
BGLY151

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL B 405
ChainResidue
BLEU43
BPHE44
BGLU45
BTRP59
BHOH513

site_idAD3
Number of Residues4
Detailsbinding site for residue GOL B 406
ChainResidue
BGLU192
BLYS320
BTHR322
BGLU327

site_idAD4
Number of Residues5
Detailsbinding site for residue ACY B 407
ChainResidue
BGLU146
BLYS174
BGLN176
BPHE177
BASN178

site_idAD5
Number of Residues8
Detailsbinding site for residue ACY B 408
ChainResidue
BLEU312
BSER313
BVAL314
BVAL315
BCYS334
BLYS335
BASP336
BGLY337

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

218500

PDB entries from 2024-04-17

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