7KCM
Full-length human mitochondrial Hsp90 (TRAP1) in complex with SdhB in the presence of AMP-PNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005164 | molecular_function | tumor necrosis factor receptor binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006457 | biological_process | protein folding |
| A | 0009386 | biological_process | translational attenuation |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0070013 | cellular_component | intracellular organelle lumen |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| A | 1901856 | biological_process | negative regulation of cellular respiration |
| A | 1903427 | biological_process | negative regulation of reactive oxygen species biosynthetic process |
| A | 1903751 | biological_process | negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005164 | molecular_function | tumor necrosis factor receptor binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006457 | biological_process | protein folding |
| B | 0009386 | biological_process | translational attenuation |
| B | 0016020 | cellular_component | membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0070013 | cellular_component | intracellular organelle lumen |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 1901856 | biological_process | negative regulation of cellular respiration |
| B | 1903427 | biological_process | negative regulation of reactive oxygen species biosynthetic process |
| B | 1903751 | biological_process | negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC |
| Chain | Residue | Details |
| C | CYS93-CYS101 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5XHZ0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q5XHZ0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQN1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 93 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQA3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
