3RNM

The crystal structure of the subunit binding of human dihydrolipoamide transacylase (E2b) bound to human dihydrolipoamide dehydrogenase (E3)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001669	cellular_component	acrosomal vesicle
A	0004148	molecular_function	dihydrolipoyl dehydrogenase (NADH) activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005929	cellular_component	cilium
A	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
A	0006099	biological_process	tricarboxylic acid cycle
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0009083	biological_process	branched-chain amino acid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0019474	biological_process	obsolete L-lysine catabolic process to acetyl-CoA
A	0031410	cellular_component	cytoplasmic vesicle
A	0031514	cellular_component	motile cilium
A	0043159	cellular_component	acrosomal matrix
A	0045252	cellular_component	oxoglutarate dehydrogenase complex
A	0045254	cellular_component	pyruvate dehydrogenase complex
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0120551	biological_process	2-oxoglutarate decarboxylation to succinyl-CoA
A	0120552	biological_process	branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
A	0160157	cellular_component	branched-chain alpha-ketoacid dehydrogenase complex
A	0160167	cellular_component	oxoadipate dehydrogenase complex
B	0001669	cellular_component	acrosomal vesicle
B	0004148	molecular_function	dihydrolipoyl dehydrogenase (NADH) activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005929	cellular_component	cilium
B	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
B	0006099	biological_process	tricarboxylic acid cycle
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0009083	biological_process	branched-chain amino acid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0019474	biological_process	obsolete L-lysine catabolic process to acetyl-CoA
B	0031410	cellular_component	cytoplasmic vesicle
B	0031514	cellular_component	motile cilium
B	0043159	cellular_component	acrosomal matrix
B	0045252	cellular_component	oxoglutarate dehydrogenase complex
B	0045254	cellular_component	pyruvate dehydrogenase complex
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0120551	biological_process	2-oxoglutarate decarboxylation to succinyl-CoA
B	0120552	biological_process	branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
B	0160157	cellular_component	branched-chain alpha-ketoacid dehydrogenase complex
B	0160167	cellular_component	oxoadipate dehydrogenase complex
C	0001669	cellular_component	acrosomal vesicle
C	0004148	molecular_function	dihydrolipoyl dehydrogenase (NADH) activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005929	cellular_component	cilium
C	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
C	0006099	biological_process	tricarboxylic acid cycle
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0009083	biological_process	branched-chain amino acid catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
C	0019474	biological_process	obsolete L-lysine catabolic process to acetyl-CoA
C	0031410	cellular_component	cytoplasmic vesicle
C	0031514	cellular_component	motile cilium
C	0043159	cellular_component	acrosomal matrix
C	0045252	cellular_component	oxoglutarate dehydrogenase complex
C	0045254	cellular_component	pyruvate dehydrogenase complex
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0120551	biological_process	2-oxoglutarate decarboxylation to succinyl-CoA
C	0120552	biological_process	branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
C	0160157	cellular_component	branched-chain alpha-ketoacid dehydrogenase complex
C	0160167	cellular_component	oxoadipate dehydrogenase complex
D	0001669	cellular_component	acrosomal vesicle
D	0004148	molecular_function	dihydrolipoyl dehydrogenase (NADH) activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005929	cellular_component	cilium
D	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
D	0006099	biological_process	tricarboxylic acid cycle
D	0006103	biological_process	2-oxoglutarate metabolic process
D	0009083	biological_process	branched-chain amino acid catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
D	0019474	biological_process	obsolete L-lysine catabolic process to acetyl-CoA
D	0031410	cellular_component	cytoplasmic vesicle
D	0031514	cellular_component	motile cilium
D	0043159	cellular_component	acrosomal matrix
D	0045252	cellular_component	oxoglutarate dehydrogenase complex
D	0045254	cellular_component	pyruvate dehydrogenase complex
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0120551	biological_process	2-oxoglutarate decarboxylation to succinyl-CoA
D	0120552	biological_process	branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
D	0160157	cellular_component	branched-chain alpha-ketoacid dehydrogenase complex
D	0160167	cellular_component	oxoadipate dehydrogenase complex
E	0016746	molecular_function	acyltransferase activity
F	0016746	molecular_function	acyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME A 500

Chain	Residue
A	SER168
A	ILE189
A	CYS277
A	ARG280
A	FAD480
A	HOH563

---

site_id	AC2
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD A 480

Chain	Residue
A	PRO16
A	GLY17
A	GLU36
A	LYS37
A	ASN38
A	GLY43
A	THR44
A	CYS45
A	VAL48
A	GLY49
A	CYS50
A	LYS54
A	GLY117
A	TYR118
A	GLY119
A	ALA147
A	THR148
A	GLY149
A	SER150
A	ILE189
A	ARG280
A	PHE283
A	GLY319
A	ASP320
A	MET326
A	LEU327
A	ALA328
A	HIS329
A	TYR359
A	HOH476
A	HOH478
A	HOH489
A	BME500
A	HOH535
A	HOH547
B	HIS452
A	ILE12
A	GLY13
A	GLY15

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NHE A 475

Chain	Residue
A	ASN225
A	GLY402
A	HOH536

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME B 500

Chain	Residue
B	SER168
B	CYS277
B	ARG280
B	FAD480

---

site_id	AC5
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD B 480

Chain	Residue
A	HIS452
A	PRO453
B	ILE12
B	GLY13
B	GLY15
B	PRO16
B	GLY17
B	ILE35
B	GLU36
B	LYS37
B	ASN38
B	GLY43
B	THR44
B	CYS45
B	VAL48
B	GLY49
B	CYS50
B	LYS54
B	TYR118
B	GLY119
B	ALA147
B	THR148
B	GLY149
B	SER150
B	ARG280
B	PHE283
B	LEU287
B	GLY319
B	ASP320
B	MET326
B	LEU327
B	ALA328
B	HIS329
B	ALA331
B	TYR359
B	BME500
B	HOH505

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NHE B 475

Chain	Residue
B	ASN225
B	GLY402
B	MET403
B	PHE474

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME C 500

Chain	Residue
C	ILE189
C	CYS277
C	GLY279
C	HOH503
C	HOH527
E	HIS160

---

site_id	AC8
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD C 480

Chain	Residue
C	ILE12
C	GLY13
C	GLY15
C	PRO16
C	GLY17
C	GLU36
C	LYS37
C	ASN38
C	GLY43
C	THR44
C	CYS45
C	VAL48
C	GLY49
C	CYS50
C	LYS54
C	GLY117
C	TYR118
C	GLY119
C	ALA147
C	THR148
C	GLY149
C	SER150
C	SER168
C	ILE189
C	ARG280
C	PHE283
C	GLY319
C	ASP320
C	MET326
C	LEU327
C	ALA328
C	HIS329
C	ALA331
C	TYR359
C	HOH476
C	HOH491
C	HOH496
C	HOH504
D	HIS452

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NHE C 475

Chain	Residue
C	ASN225
C	GLY402
C	PHE474

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME D 500

Chain	Residue
D	SER168
D	ILE189
D	CYS277
D	ARG280
D	FAD480

---

site_id	BC2
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD D 480

Chain	Residue
C	HIS452
D	ILE12
D	GLY13
D	GLY15
D	PRO16
D	GLY17
D	GLU36
D	LYS37
D	ASN38
D	GLY43
D	THR44
D	CYS45
D	VAL48
D	GLY49
D	CYS50
D	LYS54
D	TYR118
D	GLY119
D	ALA147
D	THR148
D	GLY149
D	SER150
D	SER168
D	ILE189
D	ARG280
D	PHE283
D	GLY319
D	ASP320
D	MET326
D	LEU327
D	ALA328
D	HIS329
D	TYR359
D	HOH476
D	HOH486
D	HOH489
D	HOH490
D	BME500

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NHE D 475

Chain	Residue
D	ASN225
D	PRO387
D	GLY402
D	HOH548

---

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP

Chain	Residue	Details
A	GLY42-PRO52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P09624","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	108
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15946682","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Site: {"description":"Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex","evidences":[{"source":"PubMed","id":"20385101","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	28
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6P6R2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	74
Details	Domain: {"description":"Peripheral subunit-binding (PSBD)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01170","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P53395","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P53395","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---