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6Q2P

Crystal structure of mouse viperin bound to cytidine triphosphate and S-adenosylhomocysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005789cellular_componentendoplasmic reticulum membrane
A0005811cellular_componentlipid droplet
A0051536molecular_functioniron-sulfur cluster binding
A0051607biological_processdefense response to virus
B0003824molecular_functioncatalytic activity
B0005789cellular_componentendoplasmic reticulum membrane
B0005811cellular_componentlipid droplet
B0051536molecular_functioniron-sulfur cluster binding
B0051607biological_processdefense response to virus
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SF4 A 401
ChainResidue
ACYS84
ATYR86
ACYS88
ACYS91
AGLY126
AASN158
AARG194
ASAH402

site_idAC2
Number of Residues20
Detailsbinding site for residue SAH A 402
ChainResidue
APHE92
ASER124
AGLY125
AGLY126
AGLU127
AVAL156
ASER157
AASN158
ASER180
AARG194
AASN222
AVAL224
APHE249
ACYS251
ALEU252
AASN258
AMET298
ASF4401
AHOH574
APHE90

site_idAC3
Number of Residues23
Detailsbinding site for residue CTP A 403
ChainResidue
AASN77
AHIS79
APHE92
ALYS120
AASN122
ASER124
AVAL156
ALYS220
AASN222
AARG245
ALYS247
APHE249
AMET298
ALYS299
ATYR302
AILE304
ACYS314
ALYS319
AARG347
ATYR351
AHOH520
AHOH624
AHOH682

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
ASER294
ALYS297

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 405
ChainResidue
ALYS114
BGLU164
BTRP211
BHOH873

site_idAC6
Number of Residues18
Detailsbinding site for residue B3P B 401
ChainResidue
AGLU104
APRO151
ASER354
AALA356
AASP357
AHOH557
BARG213
BASP214
BTYR215
BHOH501
BHOH502
BHOH505
BHOH528
BHOH557
BHOH581
BHOH678
BHOH754
BHOH758

site_idAC7
Number of Residues8
Detailsbinding site for residue SF4 B 402
ChainResidue
BCYS84
BTYR86
BCYS88
BCYS91
BGLY126
BASN158
BARG194
BSAH403

site_idAC8
Number of Residues20
Detailsbinding site for residue SAH B 403
ChainResidue
BMET298
BSF4402
BCTP404
BHOH596
BPHE90
BPHE92
BSER124
BGLY125
BGLY126
BGLU127
BVAL156
BSER157
BASN158
BSER180
BARG194
BASN222
BVAL224
BPHE249
BLEU252
BASN258

site_idAC9
Number of Residues24
Detailsbinding site for residue CTP B 404
ChainResidue
BASN77
BHIS79
BPHE92
BLYS120
BASN122
BSER124
BVAL156
BLYS220
BASN222
BARG245
BLYS247
BPHE249
BMET298
BLYS299
BTYR302
BILE304
BCYS314
BLYS319
BARG347
BTYR351
BSAH403
BHOH533
BHOH642
BHOH679

site_idAD1
Number of Residues3
Detailsbinding site for residue CL B 405
ChainResidue
BSER294
BLYS297
BHOH860

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28607080, ECO:0007744|PDB:5VSL, ECO:0007744|PDB:5VSM
ChainResidueDetails
ACYS84
ACYS88
ACYS91
BCYS84
BCYS88
BCYS91

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8WXG1
ChainResidueDetails
ALYS198
BLYS198

site_idSWS_FT_FI3
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q8WXG1
ChainResidueDetails
ALYS207
BLYS207

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 965
ChainResidueDetails
ACYS84metal ligand
ACYS88metal ligand
ACYS91metal ligand

site_idMCSA2
Number of Residues3
DetailsM-CSA 965
ChainResidueDetails
BCYS84metal ligand
BCYS88metal ligand
BCYS91metal ligand

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PDB entries from 2024-11-06

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