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6MAT

Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0016887molecular_functionATP hydrolysis activity
A0042254biological_processribosome biogenesis
A1990275molecular_functionpreribosome binding
B0003723molecular_functionRNA binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0016887molecular_functionATP hydrolysis activity
B0042254biological_processribosome biogenesis
B1990275molecular_functionpreribosome binding
C0003723molecular_functionRNA binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0016887molecular_functionATP hydrolysis activity
C0042254biological_processribosome biogenesis
C1990275molecular_functionpreribosome binding
D0003723molecular_functionRNA binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0016887molecular_functionATP hydrolysis activity
D0042254biological_processribosome biogenesis
D1990275molecular_functionpreribosome binding
E0003723molecular_functionRNA binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0016887molecular_functionATP hydrolysis activity
E0042254biological_processribosome biogenesis
E1990275molecular_functionpreribosome binding
F0003723molecular_functionRNA binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0016887molecular_functionATP hydrolysis activity
F0042254biological_processribosome biogenesis
F1990275molecular_functionpreribosome binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ATP A 901
ChainResidue
AHIS502
BASP630
BARG656
BARG659
APRO544
AGLY545
ACYS546
AGLY547
ALYS548
ATHR549
ALEU550
AASN645

site_idAC2
Number of Residues11
Detailsbinding site for residue ATP A 902
ChainResidue
AASP203
ASER245
AGLY246
ACYS247
AGLY248
ALYS249
ATHR250
ATHR251
AASN350
BASP331
BARG362

site_idAC3
Number of Residues12
Detailsbinding site for residue ATP B 901
ChainResidue
BHIS502
BPRO544
BGLY545
BCYS546
BGLY547
BLYS548
BTHR549
BLEU550
BASN645
CASP630
CARG656
CARG659

site_idAC4
Number of Residues13
Detailsbinding site for residue ATP B 902
ChainResidue
BASP203
BSER245
BGLY246
BCYS247
BGLY248
BLYS249
BTHR250
BTHR251
BASN350
BGLN412
CASP331
CARG334
CARG362

site_idAC5
Number of Residues12
Detailsbinding site for residue ATP C 901
ChainResidue
CHIS502
CPRO544
CGLY545
CCYS546
CGLY547
CLYS548
CTHR549
CLEU550
CASN645
DASP630
DARG656
DARG659

site_idAC6
Number of Residues12
Detailsbinding site for residue ATP C 902
ChainResidue
CASP203
CSER245
CGLY246
CCYS247
CGLY248
CLYS249
CTHR250
CTHR251
CGLN412
DASP331
DARG334
DARG362

site_idAC7
Number of Residues11
Detailsbinding site for residue ATP D 901
ChainResidue
DHIS502
DPRO544
DGLY545
DCYS546
DGLY547
DLYS548
DTHR549
DLEU550
DASN645
EARG656
EARG659

site_idAC8
Number of Residues12
Detailsbinding site for residue ATP D 902
ChainResidue
DASP203
DSER245
DGLY246
DCYS247
DGLY248
DLYS249
DTHR250
DTHR251
DGLN412
EASP331
EARG334
EARG362

site_idAC9
Number of Residues11
Detailsbinding site for residue ATP E 901
ChainResidue
EGLY248
ELYS249
ETHR250
ETHR251
EGLY408
ESER409
EGLN412
EASP203
ESER245
EGLY246
ECYS247

site_idAD1
Number of Residues4
Detailsbinding site for residue ATP F 901
ChainResidue
FGLY547
FTHR549
FLEU550
FTHR680

site_idAD2
Number of Residues10
Detailsbinding site for residue ATP F 902
ChainResidue
FASP203
FSER245
FGLY246
FCYS247
FGLY248
FLYS249
FTHR250
FTHR251
FASN350
FILE380

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues20
DetailsAAA AAA-protein family signature. VvVLaATNrpefLDpAIrrR
ChainResidueDetails
AVAL343-ARG362
AILE638-ARG656

224004

PDB entries from 2024-08-21

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