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7KLV

Full-length human mitochondrial Hsp90 (TRAP1) SpyCatcher/SpyTag-SdhB heterodimer in the presence of AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0005164molecular_functiontumor necrosis factor receptor binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005758cellular_componentmitochondrial intermembrane space
A0005759cellular_componentmitochondrial matrix
A0006457biological_processprotein folding
A0009386biological_processtranslational attenuation
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019901molecular_functionprotein kinase binding
A0051082molecular_functionunfolded protein binding
A0061077biological_processchaperone-mediated protein folding
A0071944cellular_componentcell periphery
A0140662molecular_functionATP-dependent protein folding chaperone
A1901856biological_processnegative regulation of cellular respiration
A1903427biological_processnegative regulation of reactive oxygen species biosynthetic process
A1903751biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
B0003723molecular_functionRNA binding
B0005164molecular_functiontumor necrosis factor receptor binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005654cellular_componentnucleoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005758cellular_componentmitochondrial intermembrane space
B0005759cellular_componentmitochondrial matrix
B0006099biological_processtricarboxylic acid cycle
B0006457biological_processprotein folding
B0009055molecular_functionelectron transfer activity
B0009386biological_processtranslational attenuation
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016887molecular_functionATP hydrolysis activity
B0019901molecular_functionprotein kinase binding
B0051082molecular_functionunfolded protein binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0061077biological_processchaperone-mediated protein folding
B0071944cellular_componentcell periphery
B0140662molecular_functionATP-dependent protein folding chaperone
B1901856biological_processnegative regulation of cellular respiration
B1903427biological_processnegative regulation of reactive oxygen species biosynthetic process
B1903751biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC
ChainResidueDetails
BCYS815-CYS823

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASN119
BASP158
BASN171
BPHE205
BARG402

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5XHZ0
ChainResidueDetails
BSER170

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q5XHZ0
ChainResidueDetails
BTHR174

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER194

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQN1
ChainResidueDetails
BLYS262
BLYS324
BLYS431

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS332
BLYS424
BLYS466

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BTHR494

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER568

site_idSWS_FT_FI9
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q007T0
ChainResidueDetails
BCYS815
BCYS820
BCYS823
BCYS835

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQA3
ChainResidueDetails
BLYS773
BLYS777

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PDB entries from 2024-07-24

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