Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues1
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03222","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03222","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WUM5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUM5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUM5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_03220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9Z2I9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z2I9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2I9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Z2I9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon