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5U34

Crystal structure of AacC2c1-sgRNA binary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0004519molecular_functionendonuclease activity
A0051607biological_processdefense response to virus
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: For DNase activity of RuvC domain => ECO:0000305|PubMed:27984729, ECO:0000305|PubMed:27989439
ChainResidueDetails
AASP570
AALA848
AASP977

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27984729, ECO:0000269|PubMed:27989439
ChainResidueDetails
AARG911
ASER899

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Binds DNA protospacer adjacent motif (PAM) on target DNA => ECO:0000269|PubMed:27984729
ChainResidueDetails
AASN400

site_idSWS_FT_FI4
Number of Residues10
DetailsSITE: Binds sgRNA => ECO:0000269|PubMed:27984729, ECO:0000269|PubMed:27989439
ChainResidueDetails
AARG415
AARG484
ATYR501
APHE600
AHIS614
AARG734
AGLN767
ATYR825
AGLN882
AGLN982

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Binds 'phosphate lock' on target strand DNA; via amide nitrogen => ECO:0000269|PubMed:27984729
ChainResidueDetails
AGLY478

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Binds 'phosphate lock' on target strand DNA => ECO:0000269|PubMed:27984729
ChainResidueDetails
AARG507

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Disrupts base stacking adjacent to scissile phosphate => ECO:0000305|PubMed:27984729
ChainResidueDetails
ATYR853

220472

PDB entries from 2024-05-29

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