Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1W73

Binary structure of human DECR solved by SeMet SAD.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005634	cellular_component	nucleus
A	0005739	cellular_component	mitochondrion
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	0008670	molecular_function	2,4-dienoyl-CoA reductase (NADPH) activity
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0070402	molecular_function	NADPH binding
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
A	1902494	cellular_component	catalytic complex
B	0005634	cellular_component	nucleus
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0008670	molecular_function	2,4-dienoyl-CoA reductase (NADPH) activity
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0070402	molecular_function	NADPH binding
B	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	1902494	cellular_component	catalytic complex
C	0005634	cellular_component	nucleus
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0008670	molecular_function	2,4-dienoyl-CoA reductase (NADPH) activity
C	0016491	molecular_function	oxidoreductase activity
C	0042802	molecular_function	identical protein binding
C	0070402	molecular_function	NADPH binding
C	0120162	biological_process	positive regulation of cold-induced thermogenesis
C	1902494	cellular_component	catalytic complex
D	0005634	cellular_component	nucleus
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0008670	molecular_function	2,4-dienoyl-CoA reductase (NADPH) activity
D	0016491	molecular_function	oxidoreductase activity
D	0042802	molecular_function	identical protein binding
D	0070402	molecular_function	NADPH binding
D	0120162	biological_process	positive regulation of cold-induced thermogenesis
D	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP A1330

Chain	Residue
A	GLY66
A	VAL118
A	ASN144
A	ALA145
A	ALA146
A	ILE195
A	THR196
A	LYS214
A	PRO240
A	GLY241
A	ILE243
A	THR69
A	THR245
A	HOH2045
A	HOH2073
A	HOH2128
A	HOH2129
A	HOH2130
A	HOH2131
A	HOH2132
A	GLY70
A	LEU71
A	SER90
A	ARG91
A	LYS92
A	CYS116
A	ASP117

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAP B1330

Chain	Residue
B	GLY66
B	THR69
B	GLY70
B	LEU71
B	SER90
B	ARG91
B	LYS92
B	CYS116
B	ASP117
B	VAL118
B	ASN144
B	ALA145
B	ALA146
B	ILE195
B	THR196
B	LYS214
B	GLY241
B	ILE243
B	HOH2029
B	HOH2054
B	HOH2135
B	HOH2136
B	HOH2137

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP C1330

Chain	Residue
C	GLY66
C	THR69
C	GLY70
C	LEU71
C	SER90
C	ARG91
C	LYS92
C	CYS116
C	ASP117
C	VAL118
C	ASN144
C	ALA145
C	ALA146
C	ILE195
C	THR196
C	LYS214
C	PRO240
C	GLY241
C	PRO242
C	ILE243
C	THR245
C	HOH2040
C	HOH2069
C	HOH2115
C	HOH2117
C	HOH2119

site_id	AC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAP D1330

Chain	Residue
D	HOH2135
D	HOH2136
D	HOH2137
D	HOH2138
D	HOH2139
D	GLY66
D	THR69
D	GLY70
D	LEU71
D	SER90
D	ARG91
D	LYS92
D	CYS116
D	ASP117
D	VAL118
D	ASN144
D	ALA145
D	ALA146
D	ILE195
D	THR196
D	LYS214
D	PRO240
D	GLY241
D	ILE243
D	THR245
D	HOH2026
D	HOH2078
D	HOH2134

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A1329

Chain	Residue
A	SER56
A	SER286
A	ASP287
A	HOH2127
B	LEU47

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D1328

Chain	Residue
C	MSE123
C	ASN126
D	ARG91
D	GLN115
D	ASP117
D	MSE123
D	HOH2132
D	HOH2133

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15531764","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ62","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQ62","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	VAL207
A	LYS214

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	VAL207
B	LYS214

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	VAL207
C	LYS214

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	VAL207
D	LYS214

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	LYS214
A	SER210

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	LYS214
B	SER210

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	LYS214
C	SER210

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	LYS214
D	SER210

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)