Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MDD

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	0001889	biological_process	liver development
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	0006082	biological_process	organic acid metabolic 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	0007507	biological_process	heart development
A	0009409	biological_process	response to cold
A	0009437	biological_process	carnitine metabolic process
A	0009791	biological_process	post-embryonic development
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	0042594	biological_process	response to starvation
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	0055007	biological_process	cardiac muscle cell differentiation
A	0070991	molecular_function	medium-chain fatty acyl-CoA dehydrogenase activity
B	0001889	biological_process	liver development
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	0006082	biological_process	organic acid metabolic 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	0007507	biological_process	heart development
B	0009409	biological_process	response to cold
B	0009437	biological_process	carnitine metabolic process
B	0009791	biological_process	post-embryonic development
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	0042594	biological_process	response to starvation
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	0055007	biological_process	cardiac muscle cell differentiation
B	0070991	molecular_function	medium-chain fatty acyl-CoA dehydrogenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD A 399

Chain	Residue
A	TYR133
A	THR378
A	GLN380
A	ILE384
A	HOH805
A	HOH808
A	HOH809
A	HOH810
A	HOH811
A	HOH985
B	ARG281
A	VAL135
B	THR283
B	PHE284
B	LEU288
B	HIS291
B	GLN292
B	GLN349
B	VAL350
B	GLY353
A	THR136
A	GLY141
A	SER142
A	TRP166
A	THR168
A	ILE371
A	ILE374

site_id	AC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD B 399

Chain	Residue
A	ARG281
A	THR283
A	PHE284
A	LEU288
A	HIS291
A	GLN292
A	ILE294
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	GLU376
B	THR378
B	GLN380
B	HOH855
B	HOH874
B	HOH904
B	HOH905
B	HOH906
B	HOH907

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	a catalytic site defined by CSA, PubMed 8356049

Chain	Residue	Details
A	GLU376

site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 8356049

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)