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8DYE

Crystal structure of human SDHA-SDHAF4 assembly intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005730cellular_componentnucleolus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006099biological_processtricarboxylic acid cycle
A0006105biological_processsuccinate metabolic process
A0006121biological_processmitochondrial electron transport, succinate to ubiquinone
A0007399biological_processnervous system development
A0008177molecular_functionsuccinate dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0022900biological_processelectron transport chain
A0022904biological_processrespiratory electron transport chain
A0042776biological_processproton motive force-driven mitochondrial ATP synthesis
A0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
A0050660molecular_functionflavin adenine dinucleotide binding
B0005975biological_processcarbohydrate metabolic process
B0016853molecular_functionisomerase activity
Functional Information from PROSITE/UniProt
site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
ChainResidueDetails
AARG97-GLY106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9YHT1
ChainResidueDetails
AARG340

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:32887801, ECO:0000269|PubMed:37098072, ECO:0007744|PDB:6VAX, ECO:0007744|PDB:8GS8
ChainResidueDetails
AALA69
ATHR100
AGLY105
AALA221
ASER456
ALEU457

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:32887801, ECO:0007744|PDB:6VAX
ChainResidueDetails
AALA72
AASP275
AHIS296
AARG340
AHIS407
AARG451
AALA454

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:37098072, ECO:0007744|PDB:8GS8
ChainResidueDetails
ATHR91
ALYS92
ASER98

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:37098072, ECO:0007744|PDB:6VAX, ECO:0007744|PDB:8DYD, ECO:0007744|PDB:8DYE, ECO:0007744|PDB:8GS8
ChainResidueDetails
AGLU440

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:32887801, ECO:0000269|PubMed:37098072, ECO:0007744|PDB:6VAX, ECO:0007744|PDB:8GS8
ChainResidueDetails
AHIS99

site_idSWS_FT_FI7
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8K2B3
ChainResidueDetails
ALYS167
ALYS182
ALYS480
ALYS517
ALYS550
ALYS598
ALYS624
ALYS636
ALYS647

site_idSWS_FT_FI8
Number of Residues7
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8K2B3
ChainResidueDetails
ALYS179
ALYS250
ALYS335
ALYS485
ALYS498
ALYS538
ALYS547

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:22823520
ChainResidueDetails
ATYR215

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS541
ALYS608

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K2B3
ChainResidueDetails
ALYS615

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PDB entries from 2024-10-30

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