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7MST

Phosphorylated human E105Qa GTP-specific succinyl-CoA synthetase complexed with coenzyme A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
B0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0006104biological_processsuccinyl-CoA metabolic process
B0006105biological_processsuccinate metabolic process
B0016874molecular_functionligase activity
B0019003molecular_functionGDP binding
B0032991cellular_componentprotein-containing complex
B0042709cellular_componentsuccinate-CoA ligase complex
B0044877molecular_functionprotein-containing complex binding
B0045244cellular_componentsuccinate-CoA ligase complex (GDP-forming)
B0046872molecular_functionmetal ion binding
B1901289biological_processsuccinyl-CoA catabolic process
Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues14
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GltAppgr...RMGHAG
ChainResidueDetails
AGLY248-GLY261

site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavhqttqvglGqslcVGIGGD
ChainResidueDetails
ASER160-ASP189

site_idPS01217
Number of Residues26
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIacFvNGAGLAmatcDiIflngGK
ChainResidueDetails
BGLY264-LYS289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221
ChainResidueDetails
BGLN20
BGLY53
BLEU109
BASN206
BASP220
BASN271
BGLY328

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_03221
ChainResidueDetails
BGLU42
BASP110
AILE103
ATYR167

site_idSWS_FT_FI3
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
BLYS36
BLYS95
BLYS102
BLYS163
BLYS181
BLYS234
BLYS310
BLYS349
BLYS386

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
BLYS41
BLYS301

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
BSER124
ALYS65

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS190
BLYS254

220113

PDB entries from 2024-05-22

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