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3DD6

Crystal structure of Rph, an exoribonuclease from Bacillus anthracis at 1.7 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000175molecular_function3'-5'-RNA exonuclease activity
A0003723molecular_functionRNA binding
A0006364biological_processrRNA processing
A0008033biological_processtRNA processing
A0009022molecular_functiontRNA nucleotidyltransferase activity
A0016075biological_processrRNA catabolic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0031125biological_processrRNA 3'-end processing
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG86
AGLY124
ATHR125
AARG126

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AARG86
AARG92
AARG126
AHOH549

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ATHR60
AARG99
AHOH505
AHOH520
AHOH573
ATRP58

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ALYS56
ALEU104
AGLU105
ALYS156
AGLU207
AHOH529

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 306
ChainResidue
AARG6
AARG12
AASN177
AHOH617

Functional Information from PROSITE/UniProt
site_idPS01277
Number of Residues13
DetailsRIBONUCLEASE_PH Ribonuclease PH signature. CDVIQADGGtr.TA
ChainResidueDetails
ACYS116-ALA128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00564","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19153445","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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