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2AB4

Dissecting the Roles of a Strictly Conserved Tyrosine in Substrate Recognition and Catalysis by Pseudouridine 55 Synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001522biological_processpseudouridine synthesis
A0003723molecular_functionRNA binding
A0006396biological_processRNA processing
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0009451biological_processRNA modification
A0009982molecular_functionpseudouridine synthase activity
A0016853molecular_functionisomerase activity
A0031119biological_processtRNA pseudouridine synthesis
A0140098molecular_functioncatalytic activity, acting on RNA
A0160148molecular_functiontRNA pseudouridine(55) synthase activity
A1990481biological_processmRNA pseudouridine synthesis
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 310
ChainResidue
ATYR9
ACYS43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01080
ChainResidueDetails
AASP39

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ze1
ChainResidueDetails
AASP39
APHE67

site_idMCSA1
Number of Residues4
DetailsM-CSA 56
ChainResidueDetails
AASP39covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
APHE67electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, van der waals interaction
AASP81activator, increase acidity, increase basicity, increase electrophilicity
AARG172activator, increase acidity, increase basicity, increase electrophilicity

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PDB entries from 2024-07-31

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