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1EYD

STRUCTURE OF WILD-TYPE S. NUCLEASE AT 1.7 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
Functional Information from PROSITE/UniProt
site_idPS01123
Number of Residues25
DetailsTNASE_1 Thermonuclease family signature 1. DGDTVkLmykgqpmtf.RLllVDtPE
ChainResidueDetails
AASP19-GLU43

site_idPS01284
Number of Residues11
DetailsTNASE_2 Thermonuclease family signature 2. DKYGRgLAyIY
ChainResidueDetails
AASP83-TYR93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:288045
ChainResidueDetails
AARG35
AGLU43
AARG87

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASP21
AASP40
ATHR41

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a2t
ChainResidueDetails
AARG35
AARG87

site_idMCSA1
Number of Residues6
DetailsM-CSA 165
ChainResidueDetails
AASP21metal ligand
AARG35electrostatic stabiliser, hydrogen bond donor
AASP40metal ligand
ATHR41metal ligand
AGLU43hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG87electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-11-06

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