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6G4Q

Structure of human ADP-forming succinyl-CoA ligase complex SUCLG1-SUCLA2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0006099biological_processtricarboxylic acid cycle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 401
ChainResidue
AGLN61
AGLY62
ATHR86
APRO88
AGLU131

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 402
ChainResidue
AHOH530
ALYS156
AGLY233
AASP235
AASP238

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
AGLY260
AASN261
AASN265
AHOH513
BARG175

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AGLN212
AGLN215
AHOH519
BGLU127

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
AALA126
AASN130
AGLU134
AARG154

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 406
ChainResidue
AHIS49
ATYR51
AVAL52
ATHR56
ATHR114
APRO138

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 407
ChainResidue
ALYS105
AGLU134
AALA135
AGLN150

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO B 501
ChainResidue
BGLN65
BVAL71
BPRO72
BGLY74

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
AGLY288-GLY301

site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavhqttqvglGqslcVGIGGD
ChainResidueDetails
ASER200-ASP229

site_idPS01217
Number of Residues25
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIgcLvNGAGLAmatmDiIklh.GG
ChainResidueDetails
BGLY316-GLY340

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03220
ChainResidueDetails
BLYS98
BGLY105
BASN258
BASP272
BASN323
BGLY380

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_03220
ChainResidueDetails
BASP94
BTYR162
AILE143
ATYR207

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS78
BLYS143

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
BTYR84
ALYS66

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9Z2I9
ChainResidueDetails
BLYS88
ALYS105

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2I9
ChainResidueDetails
BLYS129
BLYS139
BLYS216
BLYS368

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z2I9
ChainResidueDetails
BSER279

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Z2I9
ChainResidueDetails
BTHR341

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PDB entries from 2024-07-24

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