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7JMK

GTP-specific succinyl-CoA synthetase complexed with Mg-GDP in space group P32

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
B0006099biological_processtricarboxylic acid cycle
B0006104biological_processsuccinyl-CoA metabolic process
B0016874molecular_functionligase activity
B0042709cellular_componentsuccinate-CoA ligase complex
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
D0003824molecular_functioncatalytic activity
D0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
D0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0006099biological_processtricarboxylic acid cycle
D0006104biological_processsuccinyl-CoA metabolic process
D0016874molecular_functionligase activity
D0042709cellular_componentsuccinate-CoA ligase complex
D0046872molecular_functionmetal ion binding
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
DGLY264-LYS289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:16481318
ChainResidueDetails
DGLN20
DGLY53
DLEU109

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000305|PubMed:16481318
ChainResidueDetails
DASN206
DASP220
AILE103
CTHR24
CLYS50
CILE103

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822
ChainResidueDetails
DASN271
DGLY328

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_03221
ChainResidueDetails
DGLU42
DASP110

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
DLYS36
DLYS95
DLYS102
DLYS163
DLYS234
DLYS310
DLYS349
DLYS386

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
DLYS41
DLYS301

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
DSER124
CLYS298

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q96I99
ChainResidueDetails
DLYS190
DLYS254

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PDB entries from 2024-07-24

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