6Z5O

CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH COENZYME-A AND OXIDISED NICOTINAMIDE ADENINE DINUCLEOTIDE

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0003824	molecular_function	catalytic activity
AAA	0003857	molecular_function	3-hydroxyacyl-CoA dehydrogenase activity
AAA	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
AAA	0004300	molecular_function	enoyl-CoA hydratase activity
AAA	0005777	cellular_component	peroxisome
AAA	0005782	cellular_component	peroxisomal matrix
AAA	0005829	cellular_component	cytosol
AAA	0006629	biological_process	lipid metabolic process
AAA	0006631	biological_process	fatty acid metabolic process
AAA	0006635	biological_process	fatty acid beta-oxidation
AAA	0006636	biological_process	unsaturated fatty acid biosynthetic process
AAA	0016491	molecular_function	oxidoreductase activity
AAA	0016509	molecular_function	long-chain-3-hydroxyacyl-CoA dehydrogenase activity
AAA	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
AAA	0016829	molecular_function	lyase activity
AAA	0016853	molecular_function	isomerase activity
AAA	0016863	molecular_function	intramolecular oxidoreductase activity, transposing C=C bonds
AAA	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
AAA	0019899	molecular_function	enzyme binding
AAA	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
AAA	0036109	biological_process	alpha-linolenic acid metabolic process
AAA	0042759	biological_process	long-chain fatty acid biosynthetic process
AAA	0070403	molecular_function	NAD+ binding
AAA	1901570	biological_process	fatty acid derivative biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00067
Number of Residues	25
Details	3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. NcyGFVgNRmlaPYYnqgff.LLeeG

Chain	Residue	Details
AAA	ASN474-GLY498

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site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaIQGvalGGGlelaLgCHY

Chain	Residue	Details
AAA	LEU90-TYR110

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
AAA	GLY100

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000250

Chain	Residue	Details
AAA	GLU103
AAA	GLU123

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Blocked amino end (Ala)

Chain	Residue	Details
AAA	ALA2

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBM2

Chain	Residue	Details
AAA	LYS38
AAA	LYS721
AAA	LYS182
AAA	LYS241
AAA	LYS253
AAA	LYS279
AAA	LYS289
AAA	LYS330
AAA	LYS531
AAA	LYS576

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBM2

Chain	Residue	Details
AAA	LYS173
AAA	LYS190
AAA	LYS218
AAA	LYS275
AAA	LYS583
AAA	LYS590
AAA	LYS709

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBM2

Chain	Residue	Details
AAA	LYS249
AAA	LYS359
AAA	LYS463

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08426

Chain	Residue	Details
AAA	LYS345

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08426

Chain	Residue	Details
AAA	THR547

---