Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EXF

Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004738	molecular_function	pyruvate dehydrogenase activity
A	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005730	cellular_component	nucleolus
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006006	biological_process	glucose metabolic process
A	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
A	0006090	biological_process	pyruvate metabolic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0016491	molecular_function	oxidoreductase activity
A	0016624	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0045254	cellular_component	pyruvate dehydrogenase complex
A	0046872	molecular_function	metal ion binding
A	1902494	cellular_component	catalytic complex
B	0003824	molecular_function	catalytic activity
B	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006006	biological_process	glucose metabolic process
B	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
B	0006099	biological_process	tricarboxylic acid cycle
B	0016491	molecular_function	oxidoreductase activity
B	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
B	0045254	cellular_component	pyruvate dehydrogenase complex
B	0046872	molecular_function	metal ion binding
C	0004738	molecular_function	pyruvate dehydrogenase activity
C	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005730	cellular_component	nucleolus
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006006	biological_process	glucose metabolic process
C	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
C	0006090	biological_process	pyruvate metabolic process
C	0006099	biological_process	tricarboxylic acid cycle
C	0016491	molecular_function	oxidoreductase activity
C	0016624	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
C	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0045254	cellular_component	pyruvate dehydrogenase complex
C	0046872	molecular_function	metal ion binding
C	1902494	cellular_component	catalytic complex
D	0003824	molecular_function	catalytic activity
D	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006006	biological_process	glucose metabolic process
D	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
D	0006099	biological_process	tricarboxylic acid cycle
D	0016491	molecular_function	oxidoreductase activity
D	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
D	0045254	cellular_component	pyruvate dehydrogenase complex
D	0046872	molecular_function	metal ion binding
E	0004738	molecular_function	pyruvate dehydrogenase activity
E	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005730	cellular_component	nucleolus
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0006006	biological_process	glucose metabolic process
E	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
E	0006090	biological_process	pyruvate metabolic process
E	0006099	biological_process	tricarboxylic acid cycle
E	0016491	molecular_function	oxidoreductase activity
E	0016624	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
E	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
E	0043231	cellular_component	intracellular membrane-bounded organelle
E	0045254	cellular_component	pyruvate dehydrogenase complex
E	0046872	molecular_function	metal ion binding
E	1902494	cellular_component	catalytic complex
F	0003824	molecular_function	catalytic activity
F	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0006006	biological_process	glucose metabolic process
F	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
F	0006099	biological_process	tricarboxylic acid cycle
F	0016491	molecular_function	oxidoreductase activity
F	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
F	0045254	cellular_component	pyruvate dehydrogenase complex
F	0046872	molecular_function	metal ion binding
G	0004738	molecular_function	pyruvate dehydrogenase activity
G	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005730	cellular_component	nucleolus
G	0005739	cellular_component	mitochondrion
G	0005759	cellular_component	mitochondrial matrix
G	0006006	biological_process	glucose metabolic process
G	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
G	0006090	biological_process	pyruvate metabolic process
G	0006099	biological_process	tricarboxylic acid cycle
G	0016491	molecular_function	oxidoreductase activity
G	0016624	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
G	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
G	0043231	cellular_component	intracellular membrane-bounded organelle
G	0045254	cellular_component	pyruvate dehydrogenase complex
G	0046872	molecular_function	metal ion binding
G	1902494	cellular_component	catalytic complex
H	0003824	molecular_function	catalytic activity
H	0004739	molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005654	cellular_component	nucleoplasm
H	0005739	cellular_component	mitochondrion
H	0005759	cellular_component	mitochondrial matrix
H	0006006	biological_process	glucose metabolic process
H	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
H	0006099	biological_process	tricarboxylic acid cycle
H	0016491	molecular_function	oxidoreductase activity
H	0034604	molecular_function	pyruvate dehydrogenase (NAD+) activity
H	0045254	cellular_component	pyruvate dehydrogenase complex
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A1001

Chain	Residue
A	ASP167
A	ASN196
A	TYR198
A	TPP1003

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K D1002

Chain	Residue
D	ARG75
D	PRO111
D	ALA160
D	ILE161
D	ASP163

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE TPP A1003

Chain	Residue
A	TYR89
A	ARG90
A	GLY136
A	VAL138
A	GLY166
A	ASP167
A	GLY168
A	ALA169
A	ASN196
A	TYR198
A	GLY199
A	MET200
A	HIS263
A	MG1001
D	GLU28
D	ILE57
D	GLU59
D	PHE85
D	GLN88

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C1004

Chain	Residue
C	ASP167
C	ASN196
C	TYR198
C	TPP1006
C	HOH2002

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B1005

Chain	Residue
B	ILE112
B	ALA160
B	ILE161
B	ASP163

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE TPP C1006

Chain	Residue
B	GLU28
B	ILE57
B	GLU59
B	PHE85
B	GLN88
C	TYR89
C	ARG90
C	GLY136
C	ILE137
C	VAL138
C	GLY166
C	ASP167
C	GLY168
C	ALA169
C	ASN196
C	TYR198
C	GLY199
C	MET200
C	MG1004
C	HOH2002

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E1007

Chain	Residue
E	ASP167
E	ASN196
E	TYR198
E	TPP1009

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K H1008

Chain	Residue
H	PRO111
H	ILE112
H	VAL113
H	ALA160
H	ILE161
H	ASP163

site_id	AC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE TPP E1009

Chain	Residue
E	TYR89
E	ARG90
E	GLY136
E	VAL138
E	GLY166
E	ASP167
E	GLY168
E	ALA169
E	GLN172
E	ASN196
E	TYR198
E	GLY199
E	MET200
E	HIS263
E	MG1007
H	GLU28
H	ILE57
H	GLU59
H	PHE85
H	GLN88

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G1010

Chain	Residue
G	ASP167
G	ASN196
G	TYR198
G	TPP1012

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K F1011

Chain	Residue
F	ARG75
F	PRO111
F	ALA160
F	ILE161
F	ASP163

site_id	BC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE TPP G1012

Chain	Residue
F	PHE85
F	GLN88
G	TYR89
G	ARG90
G	GLY136
G	VAL138
G	GLY166
G	ASP167
G	GLY168
G	ALA169
G	ASN196
G	TYR198
G	GLY199
G	MET200
G	HIS263
G	MG1010
F	GLU28
F	ILE57
F	GLU59

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:12651851

Chain	Residue	Details
B	GLU59
G	LYS34
G	LYS215
G	LYS284
D	GLU59
F	GLU59
H	GLU59
C	LYS215
C	LYS284
E	LYS34
E	LYS215
E	LYS284

site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Important for interaction with DLAT => ECO:0000269\|PubMed:20160912

Chain	Residue	Details
B	ASP289
D	ASP289
F	ASP289
H	ASP289

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:Q9D051

Chain	Residue	Details
B	TYR37
D	TYR37
F	TYR37
H	TYR37
E	LYS248
E	LYS356
G	LYS248
G	LYS356

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q9D051

Chain	Residue	Details
B	LYS324
D	LYS324
F	LYS324
H	LYS324

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P35486

Chain	Residue	Details
A	SER266
C	SER266
E	SER266
G	SER266

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 => ECO:0000269\|PubMed:11486000, ECO:0000269\|PubMed:19081061

Chain	Residue	Details
A	ALA271
C	ALA271
E	ALA271
G	ALA271

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P35486

Chain	Residue	Details
A	TYR272
C	TYR272
E	TYR272
G	TYR272

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS292
C	LYS292
E	LYS292
G	LYS292

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P35486

Chain	Residue	Details
A	LYS307
C	LYS307
E	LYS307
G	LYS307

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	HIS263

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	GLU59
D	HIS128

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
F	GLU59
F	HIS128

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
H	GLU59
H	HIS128

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	HIS263

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
E	HIS263

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
G	HIS263

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	GLU59

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	GLU59

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
F	GLU59

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
H	GLU59

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	GLU59
B	HIS128

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)