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2IX0

RNase II

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0004527molecular_functionexonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006401biological_processRNA catabolic process
A0006402biological_processmRNA catabolic process
A0008408molecular_function3'-5' exonuclease activity
A0008859molecular_functionexoribonuclease II activity
A0016070biological_processRNA metabolic process
A0016078biological_processtRNA decay
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1646
ChainResidue
AASP201
AASP210
AHOH2055
AHOH2059
AHOH2060

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1647
ChainResidue
AHOH2020
AHOH2021
APRO101
AHIS103
ALEU106
AHOH2004

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE C5P A 1645
ChainResidue
APHE82
APHE86
AVAL87
APRO101
AASP102
AHIS103
AARG167

Functional Information from PROSITE/UniProt
site_idPS01175
Number of Residues25
DetailsRIBONUCLEASE_II Ribonuclease II family signature. HFGLglea.YAtWTSPIRKYgDminH
ChainResidueDetails
AHIS484-HIS508

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by PatZ => ECO:0000269|PubMed:26847092
ChainResidueDetails
ALYS501

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 338
ChainResidueDetails
AASP201metal ligand
AASP207metal ligand
AASP209activator, electrostatic stabiliser, increase nucleophilicity
AASP210metal ligand
ATYR313activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG500activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

224004

PDB entries from 2024-08-21

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