Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2NU9

C123aT Mutant of E. coli Succinyl-CoA Synthetase Orthorhombic Crystal Form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
A0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
A0016874molecular_functionligase activity
A0042709cellular_componentsuccinate-CoA ligase complex
B0000166molecular_functionnucleotide binding
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
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0006104biological_processsuccinyl-CoA metabolic process
B0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
B0016874molecular_functionligase activity
B0042709cellular_componentsuccinate-CoA ligase complex
B0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
D0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006099biological_processtricarboxylic acid cycle
D0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
D0016874molecular_functionligase activity
D0042709cellular_componentsuccinate-CoA ligase complex
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0003824molecular_functioncatalytic activity
E0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
E0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006099biological_processtricarboxylic acid cycle
E0006104biological_processsuccinyl-CoA metabolic process
E0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
E0016874molecular_functionligase activity
E0042709cellular_componentsuccinate-CoA ligase complex
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0003824molecular_functioncatalytic activity
F0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
F0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006099biological_processtricarboxylic acid cycle
F0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
F0016874molecular_functionligase activity
F0042709cellular_componentsuccinate-CoA ligase complex
G0000166molecular_functionnucleotide binding
G0000287molecular_functionmagnesium ion binding
G0003824molecular_functioncatalytic activity
G0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
G0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006099biological_processtricarboxylic acid cycle
G0006104biological_processsuccinyl-CoA metabolic process
G0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
G0016874molecular_functionligase activity
G0042709cellular_componentsuccinate-CoA ligase complex
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0003824molecular_functioncatalytic activity
H0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
H0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
H0005515molecular_functionprotein binding
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0006099biological_processtricarboxylic acid cycle
H0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
H0016874molecular_functionligase activity
H0042709cellular_componentsuccinate-CoA ligase complex
I0000166molecular_functionnucleotide binding
I0000287molecular_functionmagnesium ion binding
I0003824molecular_functioncatalytic activity
I0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
I0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
I0005515molecular_functionprotein binding
I0005524molecular_functionATP binding
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0006099biological_processtricarboxylic acid cycle
I0006104biological_processsuccinyl-CoA metabolic process
I0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
I0016874molecular_functionligase activity
I0042709cellular_componentsuccinate-CoA ligase complex
I0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 389
ChainResidue
BGLY53
BARG54
BGLY55
BASP213
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 390
ChainResidue
AARG243
BMET1
BGLY220
BARG233
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 389
ChainResidue
EGLY53
EARG54
EGLY55
EASP213
EGLY52
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 390
ChainResidue
DARG243
EMET1
EGLY220
EARG233
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 G 389
ChainResidue
GGLY52
GGLY53
GARG54
GGLY55
GASP213
site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 G 390
ChainResidue
FARG243
GMET1
GGLY220
GARG233
site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 I 389
ChainResidue
IGLY52
IGLY53
IARG54
IGLY55
IASP213
site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 I 390
ChainResidue
HARG243
IMET1
IGLY220
IARG233
site_idAC9
Number of Residues22
DetailsBINDING SITE FOR RESIDUE COA A 300
ChainResidue
ATHR16
AGLY17
ASER18
AGLN19
AVAL38
ATHR39
APRO40
ALYS42
ATYR71
AVAL72
APRO73
AILE95
ATHR96
AGLU97
AASN122
ATHR123
APRO124
AILE136
ANEP246
EGLU33
ESER36
ELYS66
site_idBC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE COA D 301
ChainResidue
BGLU33
BSER36
BLYS66
DGLY14
DTHR16
DGLY17
DSER18
DGLN19
DTHR39
DLYS42
DTYR71
DVAL72
DPRO73
DILE95
DTHR96
DGLU97
DTHR123
DPRO124
DILE136
IARG161
site_idBC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE COA F 400
ChainResidue
IGLU33
ISER36
ILYS66
BARG161
FGLY14
FTHR16
FGLY17
FSER18
FGLN19
FVAL38
FTHR39
FPRO40
FLYS42
FTYR71
FVAL72
FPRO73
FSER80
FILE95
FTHR96
FGLU97
FASN122
FTHR123
FILE136
FNEP246
IARG29
site_idBC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE COA H 401
ChainResidue
GARG29
GGLU33
GSER36
GLYS66
HTHR16
HGLY17
HSER18
HGLN19
HTHR39
HPRO40
HLYS42
HTYR71
HVAL72
HPRO73
HILE95
HTHR96
HGLU97
HASN122
HTHR123
HPRO124
Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues14
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GvtApkgk...RMGHAG
ChainResidueDetails
AGLY235-GLY248
site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavkqttdygfGqstcVGIGGD
ChainResidueDetails
ASER151-ASP180
site_idPS01217
Number of Residues26
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIgcMvNGAGLAmgtmDiVklhgGE
ChainResidueDetails
BGLY257-GLU282
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01988","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11781092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9917402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01988","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10625475","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11781092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8144675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9917402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01988","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues940
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_00558","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00558","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10625475","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00558","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cqj
ChainResidueDetails
AGLU208
BTYR109
BGLU197
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cqj
ChainResidueDetails
DGLU208
ETYR109
EGLU197
site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cqj
ChainResidueDetails
FGLU208
GTYR109
GGLU197
site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cqj
ChainResidueDetails
HGLU208
ITYR109
IGLU197
site_idMCSA1
Number of Residues2
DetailsM-CSA 476
ChainResidueDetails
BTYR109electrostatic stabiliser, steric role
BGLU197electrostatic stabiliser, modifies pKa
site_idMCSA2
Number of Residues2
DetailsM-CSA 476
ChainResidueDetails
DVAL109electrostatic stabiliser, steric role
DASP197electrostatic stabiliser, modifies pKa
site_idMCSA3
Number of Residues2
DetailsM-CSA 476
ChainResidueDetails
FVAL109electrostatic stabiliser, steric role
FASP197electrostatic stabiliser, modifies pKa
site_idMCSA4
Number of Residues2
DetailsM-CSA 476
ChainResidueDetails
HVAL109electrostatic stabiliser, steric role
HASP197electrostatic stabiliser, modifies pKa

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon