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3HAX

Crystal structure of a substrate-bound Gar1-minus H/ACA RNP from Pyrococcus furiosus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000495biological_processbox H/ACA sno(s)RNA 3'-end processing
A0001522biological_processpseudouridine synthesis
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0006396biological_processRNA processing
A0008033biological_processtRNA processing
A0009451biological_processRNA modification
A0009982molecular_functionpseudouridine synthase activity
A0016853molecular_functionisomerase activity
A0031118biological_processrRNA pseudouridine synthesis
A0031119biological_processtRNA pseudouridine synthesis
A0031120biological_processsnRNA pseudouridine synthesis
A0160148molecular_functiontRNA pseudouridine(55) synthase activity
A1990481biological_processmRNA pseudouridine synthesis
C0001522biological_processpseudouridine synthesis
C0005515molecular_functionprotein binding
C0006364biological_processrRNA processing
C0030515molecular_functionsnoRNA binding
C0042254biological_processribosome biogenesis
C1990904cellular_componentribonucleoprotein complex
D0001682biological_processtRNA 5'-leader removal
D0003723molecular_functionRNA binding
D0003735molecular_functionstructural constituent of ribosome
D0004526molecular_functionribonuclease P activity
D0005737cellular_componentcytoplasm
D0005840cellular_componentribosome
D0006364biological_processrRNA processing
D0006412biological_processtranslation
D0008033biological_processtRNA processing
D0019843molecular_functionrRNA binding
D0042254biological_processribosome biogenesis
D1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGE A 401
ChainResidue
AGLU44
ATRP230
ALYS231
AGLY234
DARG46
DHOH521
EG21
EG22

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE A 402
ChainResidue
ATRP257
ALYS279
ALEU295
AASP297
CPRO21
AVAL21

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AGLU134

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 201
ChainResidue
CCYS8
CCYS11
CCYS20
CCYS23

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 C 401
ChainResidue
CARG34
DGLU62
DHIS66

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO D 401
ChainResidue
DGLY106
DLYS107

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 200
ChainResidue
EHOH401
EHOH402
EHOH403
EHOH404
EHOH405
EHOH406

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 201
ChainResidue
DASP110
DGLU113
EHOH411
EHOH412
EHOH413
EHOH414

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 202
ChainResidue
CGLU43
EC37
EHOH421
EHOH422
EHOH423
EHOH424

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG E 203
ChainResidue
EHOH431
EHOH432
EHOH433

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG E 204
ChainResidue
EHOH441
EHOH442
EHOH443
EHOH444

Functional Information from PROSITE/UniProt
site_idPS01082
Number of Residues18
DetailsRIBOSOMAL_L7AE Ribosomal protein L7Ae signature. CeekeIPYiyVpSKkeLG
ChainResidueDetails
DCYS71-GLY88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01081
ChainResidueDetails
AASP85

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ze1
ChainResidueDetails
AASP85
ATYR113

237423

PDB entries from 2025-06-11

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