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5RSA

COMPARISON OF TWO INDEPENDENTLY REFINED MODELS OF RIBONUCLEASE-A

Replaces:  4RSAReplaces:  2RSAReplaces:  3RSA
Functional Information from GO Data
ChainGOidnamespacecontents
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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 125
ChainResidue
AGLN11
AHIS12
ALYS41
AHIS119
APHE120
ADOD160

site_idACT
Number of Residues9
DetailsACTIVE SITE OF ENZYME
ChainResidue
AHIS12
ALYS41
AVAL43
AASN44
ATHR45
AHIS119
APHE120
AASP121
ASER123

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 acceptor
ChainResidueDetails
AHIS12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS119

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS7
AARG10
ALYS41
ALYS66
AARG85

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761
ChainResidueDetails
ALYS1
ALYS7
ALYS37
ALYS41

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553
ChainResidueDetails
AASN34

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 164
ChainResidueDetails
AHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS41electrostatic stabiliser, hydrogen bond donor
AHIS119hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APHE120electrostatic stabiliser, hydrogen bond donor
AASP121electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-04-24

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