3B96

Structural Basis for Substrate Fatty-Acyl Chain Specificity: Crystal Structure of Human Very-Long-Chain Acyl-CoA Dehydrogenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000062	molecular_function	fatty-acyl-CoA binding
A	0001659	biological_process	temperature homeostasis
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0004466	molecular_function	long-chain fatty acyl-CoA dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005759	cellular_component	mitochondrial matrix
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0015980	biological_process	energy derivation by oxidation of organic compounds
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0017099	molecular_function	very-long-chain fatty acyl-CoA dehydrogenase activity
A	0030855	biological_process	epithelial cell differentiation
A	0031966	cellular_component	mitochondrial membrane
A	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
A	0042645	cellular_component	mitochondrial nucleoid
A	0042802	molecular_function	identical protein binding
A	0045717	biological_process	negative regulation of fatty acid biosynthetic process
A	0046322	biological_process	negative regulation of fatty acid oxidation
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0090181	biological_process	regulation of cholesterol metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MYA A 1

Chain	Residue
A	TYR120
A	HOH1002
A	VAL124
A	GLY135
A	ILE144
A	LEU297
A	PHE421
A	GLU422
A	GLY423
A	FAD616

---

site_id	AC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD A 616

Chain	Residue
A	MYA1
A	PHE174
A	LEU176
A	THR177
A	GLY182
A	SER183
A	TRP209
A	ILE210
A	SER211
A	ARG326
A	GLN328
A	PHE329
A	ILE333
A	PHE336
A	GLN395
A	ILE396
A	GLY399
A	ILE417
A	PHE421
A	THR424
A	ASP426
A	ILE427
A	GLN522
A	HOH639
A	HOH654
A	HOH668
A	HOH680

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS175-SER187

---

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

Chain	Residue	Details
A	GLN395-ASP414

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18227065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9461620","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2UXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B96","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18227065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2UXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B96","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50544","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

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	GLY300

---

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

Chain	Residue	Details
A	GLU422

---