Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3MWQ

Crystal structure of ribonuclease A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 257
ChainResidue
ALYS133
ATHR135
AALA136
AHOH280

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 258
ChainResidue
AHOH290
AGLN143
AHIS144
ALYS173
AHIS251
APHE252

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 259
ChainResidue
AGLN11
AHIS12
AHIS119
APHE120
AHOH319

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 260
ChainResidue
ATHR3
AALA4
AARG130
AASN194
ATYR205
AHOH321

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 261
ChainResidue
ALYS198
AASP253
AALA254
AALA254
ASER255
AHOH267
AHOH377

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 262
ChainResidue
AHIS12
ALYS41
AVAL43
AASN44
ATHR45
AGOL263
AHOH495

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 263
ChainResidue
ALYS1
ALYS66
AALA122
ASER123
AGOL262
AHOH450
AHOH469
AHOH493

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF
ChainResidueDetails
ACYS40-PHE46
ACYS172-PHE178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"4030761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","featureId":"CAR_000006","evidences":[{"source":"PubMed","id":"19358553","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 164
ChainResidueDetails
AHIS144hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS173electrostatic stabiliser, hydrogen bond donor
AHIS251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APHE252electrostatic stabiliser, hydrogen bond donor
AASP253electrostatic stabiliser, hydrogen bond acceptor

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon