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3EV6

Crystal Structure of Ribonuclease A in 50% R,S,R-Bisfuranol

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0050830biological_processdefense response to Gram-positive bacterium
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0004522molecular_functionribonuclease A activity
B0004540molecular_functionRNA nuclease activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0016829molecular_functionlyase activity
B0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RSF A 917
ChainResidue
ASER23
AASN24
ASER50
ALEU51
AALA52

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE RSF A 918
ChainResidue
ASER89
ALYS91

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RSF B 907
ChainResidue
BARG10
BASN34
BHOH959
ATYR76
BGLU2

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RSF B 919
ChainResidue
ASER59
AGLN60
AHOH920
BGLU9
BMET13
BASP14
BSER15
BLEU51
BHOH929
BHOH1012

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RSF B 920
ChainResidue
ATHR70
BGLU49
BHOH964
BHOH1009

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RSF B 921
ChainResidue
ALYS61
AVAL63
AASN113
AHOH964
AHOH984
BALA56
BSER59
BHOH936
BHOH981
BHOH1053

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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS12
BHIS12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS119
BHIS119

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ALYS7
AARG10
BLYS66
BARG85
ALYS41
ALYS66
AARG85
BLYS7
BARG10
BLYS41

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761
ChainResidueDetails
ALYS1
ALYS7
ALYS37
ALYS41
BLYS1
BLYS7
BLYS37
BLYS41

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553
ChainResidueDetails
AASN34
BASN34

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

site_idMCSA2
Number of Residues5
DetailsM-CSA 164
ChainResidueDetails
BHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLYS41electrostatic stabiliser, hydrogen bond donor
BHIS119hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPHE120electrostatic stabiliser, hydrogen bond donor
BASP121electrostatic stabiliser, hydrogen bond acceptor

221051

PDB entries from 2024-06-12

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