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3MWT

Crystal structure of Lassa fever virus nucleoprotein in complex with Mn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0008408molecular_function3'-5' exonuclease activity
A0016787molecular_functionhydrolase activity
A0019013cellular_componentviral nucleocapsid
A0019029cellular_componenthelical viral capsid
A0019049biological_processvirus-mediated perturbation of host defense response
A0030430cellular_componenthost cell cytoplasm
A0039548biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
A0039689biological_processnegative stranded viral RNA replication
A0039696biological_processRNA-templated viral transcription
A0039724biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A1990904cellular_componentribonucleoprotein complex
B0003723molecular_functionRNA binding
B0008408molecular_function3'-5' exonuclease activity
B0016787molecular_functionhydrolase activity
B0019013cellular_componentviral nucleocapsid
B0019029cellular_componenthelical viral capsid
B0019049biological_processvirus-mediated perturbation of host defense response
B0030430cellular_componenthost cell cytoplasm
B0039548biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
B0039689biological_processnegative stranded viral RNA replication
B0039696biological_processRNA-templated viral transcription
B0039724biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B1990904cellular_componentribonucleoprotein complex
C0003723molecular_functionRNA binding
C0008408molecular_function3'-5' exonuclease activity
C0016787molecular_functionhydrolase activity
C0019013cellular_componentviral nucleocapsid
C0019029cellular_componenthelical viral capsid
C0019049biological_processvirus-mediated perturbation of host defense response
C0030430cellular_componenthost cell cytoplasm
C0039548biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
C0039689biological_processnegative stranded viral RNA replication
C0039696biological_processRNA-templated viral transcription
C0039724biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 680
ChainResidue
AASP389
AGLU391
AASP533

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 690
ChainResidue
AGLU399
AHIS412
ACYS506
AHIS509
ACYS529

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN B 680
ChainResidue
BGLU391
BASP533
BASP389

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 690
ChainResidue
BGLU399
BHIS412
BCYS506
BHIS509
BCYS529

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN C 680
ChainResidue
CASP389
CGLU391
CASP533

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 690
ChainResidue
CGLU399
CCYS506
CHIS509
CCYS529

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
ChainResidueDetails
AASP389
AGLU391
AASP533
BASP389
BGLU391
BASP533
CASP389
CGLU391
CASP533

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
ChainResidueDetails
AGLU399
CCYS506
CHIS509
CCYS529
ACYS506
AHIS509
ACYS529
BGLU399
BCYS506
BHIS509
BCYS529
CGLU399

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Important for exonuclease activity => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117
ChainResidueDetails
AASP466
BASP466
CASP466

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PDB entries from 2024-11-06

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