Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MDE

CRYSTAL STRUCTURES OF MEDIUM CHAIN ACYL-COA DEHYDROGENASE FROM PIG LIVER MITOCHONDRIA WITH AND WITHOUT SUBSTRATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005978	biological_process	glycogen biosynthetic process
A	0006111	biological_process	regulation of gluconeogenesis
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0019254	biological_process	carnitine metabolic process, CoA-linked
A	0030424	cellular_component	axon
A	0031966	cellular_component	mitochondrial membrane
A	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
A	0042802	molecular_function	identical protein binding
A	0045329	biological_process	carnitine biosynthetic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051791	biological_process	medium-chain fatty acid metabolic process
A	0051793	biological_process	medium-chain fatty acid catabolic process
A	0070991	molecular_function	medium-chain fatty acyl-CoA dehydrogenase activity
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005978	biological_process	glycogen biosynthetic process
B	0006111	biological_process	regulation of gluconeogenesis
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0019254	biological_process	carnitine metabolic process, CoA-linked
B	0030424	cellular_component	axon
B	0031966	cellular_component	mitochondrial membrane
B	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
B	0042802	molecular_function	identical protein binding
B	0045329	biological_process	carnitine biosynthetic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051791	biological_process	medium-chain fatty acid metabolic process
B	0051793	biological_process	medium-chain fatty acid catabolic process
B	0070991	molecular_function	medium-chain fatty acyl-CoA dehydrogenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CO8 A 400

Chain	Residue
A	THR96
A	MET249
A	PHE252
A	ASP253
A	ARG256
A	ARG324
A	THR326
A	TYR375
A	GLU376
A	GLY377
A	ILE381
A	GLU99
A	FAD399
A	HOH803
A	HOH845
A	HOH860
A	HOH868
A	HOH888
A	HOH986
A	LEU103
A	GLY141
A	SER142
A	VAL144
A	ALA145
A	SER191
A	PHE245

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CO8 B 400

Chain	Residue
B	THR96
B	GLU99
B	LEU103
B	GLY141
B	SER142
B	VAL144
B	SER191
B	PHE245
B	MET249
B	PHE252
B	THR326
B	TYR375
B	GLU376
B	GLY377
B	FAD399
B	HOH946
B	HOH960

site_id	AC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD A 399

Chain	Residue
A	TYR133
A	VAL135
A	THR136
A	GLY141
A	SER142
A	TRP166
A	ILE167
A	THR168
A	ILE371
A	ILE374
A	THR378
A	GLN380
A	CO8400
A	HOH802
A	HOH804
A	HOH805
A	HOH846
A	HOH850
B	ARG281
B	THR283
B	PHE284
B	LEU288
B	GLN292
B	ILE294
B	GLN349
B	VAL350
B	GLY353
B	HOH806

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD B 399

Chain	Residue
A	ARG281
A	THR283
A	PHE284
A	LEU288
A	HIS291
A	GLN292
A	GLN349
A	VAL350
A	GLY353
B	TYR133
B	VAL135
B	THR136
B	GLY141
B	SER142
B	TRP166
B	THR168
B	ILE371
B	ILE374
B	TYR375
B	THR378
B	GLN380
B	CO8400
B	HOH901
B	HOH903
B	HOH904
B	HOH925
B	HOH926

Functional Information from PROSITE/UniProt

site_id	PS00072
Number of Residues	13
Details	ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CVTEpgAGSDvaG

Chain	Residue	Details
A	CYS134-GLY146

site_id	PS00073
Number of Residues	20
Details	ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QvFGGnGFntEypveKlmrD

Chain	Residue	Details
A	GLN349-ASP368

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12966080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8356049","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12966080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8356049","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8356049","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MDE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12966080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8356049","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8356049","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11310","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	THR255

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

Chain	Residue	Details
B	THR255

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

Chain	Residue	Details
A	GLU376

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

Chain	Residue	Details
B	GLU376

site_id	MCSA1
Number of Residues	1
Details	M-CSA 893

Chain	Residue	Details
A	GLU376	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	1
Details	M-CSA 893

Chain	Residue	Details
B	GLU376	proton shuttle (general acid/base)

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)