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6MV6

Crystal structure of RNAse 6

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0006401biological_processRNA catabolic process
A0006952biological_processdefense response
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0031410cellular_componentcytoplasmic vesicle
A0042742biological_processdefense response to bacterium
A0045087biological_processinnate immune response
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051607biological_processdefense response to virus
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 A 201
ChainResidue
ASER59
AGLN110
ALYS111
AHOH315
AHOH339
AHOH343
AHOH372
AHOH375

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 A 202
ChainResidue
AHIS15
AHIS122
ALEU123
AHOH307
AHOH368
AGLN14

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 A 203
ChainResidue
AHIS36
AARG66
AHIS67
ASER112
AHOH308
AHOH355

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKhqNTF
ChainResidueDetails
ACYS37-PHE43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q64438","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q64438","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for bactericidal activity, bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS)","evidences":[{"source":"PubMed","id":"27089320","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Facilitates cleavage of polynucleotide substrates","evidences":[{"source":"PubMed","id":"27013146","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Critical for catalytic activity","evidences":[{"source":"UniProtKB","id":"Q9H1E1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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