Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1DJ0

THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 600
ChainResidue
AHIS202
AVAL204
AARG205
AHOH741

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 601
ChainResidue
BHIS202
BVAL204
BARG205
BHOH658

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsRegion: {"description":"RNA binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsRegion: {"description":"Interaction with tRNA","evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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 Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Interaction with tRNA; Important for base-flipping","evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsSite: {"description":"Interaction with tRNA","evidences":[{"source":"PubMed","id":"17466622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11976723, 12581659, 20091078
ChainResidueDetails
AASP60

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11976723, 12581659, 20091078
ChainResidueDetails
BASP60

site_idMCSA1
Number of Residues3
DetailsM-CSA 493
ChainResidueDetails
AARG58electrostatic stabiliser
AASP60covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AARG205electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 493
ChainResidueDetails
BARG58electrostatic stabiliser
BASP60covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BARG205electrostatic stabiliser

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon