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2NQP

Crystal structure of pseudoudirinde synthase TruA in complex with leucyl tRNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0001522biological_processpseudouridine synthesis
A0003723molecular_functionRNA binding
A0006396biological_processRNA processing
A0008033biological_processtRNA processing
A0009451biological_processRNA modification
A0009982molecular_functionpseudouridine synthase activity
A0016853molecular_functionisomerase activity
A0031119biological_processtRNA pseudouridine synthesis
A0042803molecular_functionprotein homodimerization activity
A0106029molecular_functiontRNA pseudouridine synthase activity
A0140098molecular_functioncatalytic activity, acting on RNA
A0160147molecular_functiontRNA pseudouridine(38-40) synthase activity
B0000049molecular_functiontRNA binding
B0001522biological_processpseudouridine synthesis
B0003723molecular_functionRNA binding
B0006396biological_processRNA processing
B0008033biological_processtRNA processing
B0009451biological_processRNA modification
B0009982molecular_functionpseudouridine synthase activity
B0016853molecular_functionisomerase activity
B0031119biological_processtRNA pseudouridine synthesis
B0042803molecular_functionprotein homodimerization activity
B0106029molecular_functiontRNA pseudouridine synthase activity
B0140098molecular_functioncatalytic activity, acting on RNA
B0160147molecular_functiontRNA pseudouridine(38-40) synthase activity
C0000049molecular_functiontRNA binding
C0001522biological_processpseudouridine synthesis
C0003723molecular_functionRNA binding
C0006396biological_processRNA processing
C0008033biological_processtRNA processing
C0009451biological_processRNA modification
C0009982molecular_functionpseudouridine synthase activity
C0016853molecular_functionisomerase activity
C0031119biological_processtRNA pseudouridine synthesis
C0042803molecular_functionprotein homodimerization activity
C0106029molecular_functiontRNA pseudouridine synthase activity
C0140098molecular_functioncatalytic activity, acting on RNA
C0160147molecular_functiontRNA pseudouridine(38-40) synthase activity
D0000049molecular_functiontRNA binding
D0001522biological_processpseudouridine synthesis
D0003723molecular_functionRNA binding
D0006396biological_processRNA processing
D0008033biological_processtRNA processing
D0009451biological_processRNA modification
D0009982molecular_functionpseudouridine synthase activity
D0016853molecular_functionisomerase activity
D0031119biological_processtRNA pseudouridine synthesis
D0042803molecular_functionprotein homodimerization activity
D0106029molecular_functiontRNA pseudouridine synthase activity
D0140098molecular_functioncatalytic activity, acting on RNA
D0160147molecular_functiontRNA pseudouridine(38-40) synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K F 77
ChainResidue
FU60
FC62

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K F 78
ChainResidue
FG49
FG59

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K F 79
ChainResidue
FU54
FU55

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K C 271
ChainResidue
CALA89

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K F 80
ChainResidue
FK81
FU20
FA20

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K F 81
ChainResidue
FU20
FU48
FG59
FU60
FK80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsRegion: {"description":"RNA binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsRegion: {"description":"Interaction with tRNA","evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10588695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9425056","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Interaction with tRNA; Important for base-flipping","evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsSite: {"description":"Interaction with tRNA","evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dj0
ChainResidueDetails
AASP60

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dj0
ChainResidueDetails
BASP60

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dj0
ChainResidueDetails
CASP60

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dj0
ChainResidueDetails
DASP60

site_idMCSA1
Number of Residues3
DetailsM-CSA 493
ChainResidueDetails
BARG58electrostatic stabiliser
BASP60covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BARG205electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 493
ChainResidueDetails
CARG58electrostatic stabiliser
CASP60covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
CARG205electrostatic stabiliser

site_idMCSA3
Number of Residues3
DetailsM-CSA 493
ChainResidueDetails
DARG58electrostatic stabiliser
DASP60covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
DARG205electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 493
ChainResidueDetails

243531

PDB entries from 2025-10-22

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