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4X09

Structure of human RNase 6 in complex with sulphate anions

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0006401biological_processRNA catabolic process
A0006952biological_processdefense response
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 SO4 A 301
ChainResidue
AGLN14
AHIS15
AHIS122
ALEU123
AHOH415
AHOH422
AHOH437
AHOH470

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG66
AHIS67
AHOH403
AHOH425
AHIS36

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG25
AARG92
AHOH423
AHOH479

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 304
ChainResidue
AHIS36
AHIS39
AARG66
AHOH438
AHOH459
AHOH480

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 305
ChainResidue
ASER59
AGLN110
ALYS111
AHOH401
AHOH477

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
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q64438
ChainResidueDetails
AHIS15

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q64438
ChainResidueDetails
AHIS122

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS38
ALYS63
AARG82

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for bactericidal activity, bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS) => ECO:0000269|PubMed:27089320
ChainResidueDetails
ATRP1
AILE13

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Facilitates cleavage of polynucleotide substrates => ECO:0000269|PubMed:27013146
ChainResidueDetails
AHIS36

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Critical for catalytic activity => ECO:0000250|UniProtKB:Q9H1E1
ChainResidueDetails
ALYS38

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN32
AASN77

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PDB entries from 2024-05-01

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