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1SRN

THE REFINED CRYSTAL STRUCTURE OF A FULLY ACTIVE SEMISYNTHETIC RIBONUCLEASE AT 1.8 ANGSTROMS RESOLUTION

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 125
ChainResidue
AGLN11
AHIS12
ALYS41
AHOH138
AHOH153
AHOH228
BHIS119
BPHE120

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
BHIS119

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS7
AARG10
ALYS41
ALYS66
AARG85

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761
ChainResidueDetails
ALYS1
ALYS7
ALYS37
ALYS41

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553
ChainResidueDetails
AASN34

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 164
ChainResidueDetails
BHIS119hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPHE120electrostatic stabiliser, hydrogen bond donor
BASP121electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-04-24

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