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3NUC

STAPHLOCOCCAL NUCLEASE, 1-N-PROPANE THIOL DISULFIDE TO V23C VARIANT

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 150
ChainResidue
AASP21
AASP40
ATHR41
ATHP151
AHOH208
AHOH214
AHOH252

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE THP A 151
ChainResidue
AASP40
ALYS71
AASP83
ALYS84
ATYR85
AARG87
ALEU89
ATYR113
ATYR115
ACA150
AHOH202
AHOH208
AHOH211
AHOH217
AHOH220
AHOH237
AHOH251
AHOH252
AARG35
ALEU36

Functional Information from PROSITE/UniProt
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 2024-11-13

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