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1XPI

Crystal structure of the catalytic domain of E. coli pseudouridine synthase RluC

Functional Information from GO Data
ChainGOidnamespacecontents
A0001522biological_processpseudouridine synthesis
A0003723molecular_functionRNA binding
A0009451biological_processRNA modification
A0009982molecular_functionpseudouridine synthase activity
B0001522biological_processpseudouridine synthesis
B0003723molecular_functionRNA binding
B0009451biological_processRNA modification
B0009982molecular_functionpseudouridine synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 401
ChainResidue
AHIS114
AILE124
AARG128
ALYS189
AHOH665
AHOH666

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 402
ChainResidue
ASER186
ALYS197
AILE199
AARG205
AARG225
AARG142
ATRP184
AGLN185

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 403
ChainResidue
AASP144
AGLU204
AARG205
AHIS242
AHOH580

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 404
ChainResidue
APRO303
AMET304
ALYS309
BARG161
BHOH596

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 405
ChainResidue
BLEU195
BLYS197
BLYS214
BARG240
BTHR241

Functional Information from PROSITE/UniProt
site_idPS01129
Number of Residues15
DetailsPSI_RLU Rlu family of pseudouridine synthase signature. VHRLDrdTSGVLLVA
ChainResidueDetails
AVAL140-ALA154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:18820021
ChainResidueDetails
AASP144
BASP144

221371

PDB entries from 2024-06-19

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