Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CYD

CARBONYL REDUCTASE COMPLEXED WITH NADPH AND 2-PROPANOL

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004090	molecular_function	carbonyl reductase (NADPH) activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005997	biological_process	xylulose metabolic process
A	0006006	biological_process	glucose metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0042802	molecular_function	identical protein binding
A	0050038	molecular_function	L-xylulose reductase (NADPH) activity
B	0004090	molecular_function	carbonyl reductase (NADPH) activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005997	biological_process	xylulose metabolic process
B	0006006	biological_process	glucose metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0042802	molecular_function	identical protein binding
B	0050038	molecular_function	L-xylulose reductase (NADPH) activity
C	0004090	molecular_function	carbonyl reductase (NADPH) activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005997	biological_process	xylulose metabolic process
C	0006006	biological_process	glucose metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0042802	molecular_function	identical protein binding
C	0050038	molecular_function	L-xylulose reductase (NADPH) activity
D	0004090	molecular_function	carbonyl reductase (NADPH) activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005997	biological_process	xylulose metabolic process
D	0006006	biological_process	glucose metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0042802	molecular_function	identical protein binding
D	0050038	molecular_function	L-xylulose reductase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NDP A 245

Chain	Residue
A	GLY14
A	ASP60
A	LEU61
A	ASN83
A	ALA85
A	ARG102
A	VAL106
A	VAL134
A	SER135
A	SER136
A	TYR149
A	GLY16
A	LYS153
A	PRO179
A	THR180
A	VAL181
A	VAL182
A	THR184
A	MET186
A	GLY187
A	IPA246
A	HOH250
A	LYS17
A	HOH283
A	HOH284
A	HOH302
A	HOH311
A	HOH347
A	HOH361
A	GLY18
A	ILE19
A	THR38
A	ARG39
A	THR40
A	VAL59

site_id	AC2
Number of Residues	37
Details	BINDING SITE FOR RESIDUE NDP B 245

Chain	Residue
B	GLY14
B	GLY16
B	LYS17
B	GLY18
B	ILE19
B	THR38
B	ARG39
B	THR40
B	VAL59
B	ASP60
B	LEU61
B	ASN83
B	ALA84
B	ALA85
B	ARG102
B	VAL106
B	VAL134
B	SER135
B	SER136
B	TYR149
B	LYS153
B	PRO179
B	THR180
B	VAL181
B	VAL182
B	THR184
B	ASP185
B	MET186
B	GLY187
B	IPA246
B	HOH247
B	HOH273
B	HOH301
B	HOH314
B	HOH388
B	HOH391
B	HOH393

site_id	AC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NDP C 245

Chain	Residue
C	HOH280
C	HOH285
C	HOH293
C	HOH305
C	HOH382
C	GLY14
C	GLY16
C	LYS17
C	GLY18
C	ILE19
C	THR38
C	ARG39
C	THR40
C	VAL59
C	ASP60
C	LEU61
C	ASN83
C	ALA85
C	VAL106
C	VAL134
C	SER135
C	TYR149
C	LYS153
C	PRO179
C	THR180
C	VAL181
C	VAL182
C	THR184
C	MET186
C	GLY187
C	IPA246
C	HOH248

site_id	AC4
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NDP D 245

Chain	Residue
D	GLY14
D	GLY16
D	LYS17
D	GLY18
D	ILE19
D	THR38
D	ARG39
D	THR40
D	VAL59
D	ASP60
D	LEU61
D	ASN83
D	ALA85
D	VAL106
D	VAL134
D	SER135
D	SER136
D	TYR149
D	LYS153
D	PRO179
D	THR180
D	VAL181
D	VAL182
D	THR184
D	MET186
D	GLY187
D	IPA246
D	HOH248
D	HOH253
D	HOH340
D	HOH353
D	HOH364
D	HOH394

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA A 246

Chain	Residue
A	SER136
A	LEU146
A	TYR149
A	VAL190
A	NDP245

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA B 246

Chain	Residue
B	SER136
B	TYR149
B	NDP245

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA C 246

Chain	Residue
C	SER136
C	TYR149
C	NDP245

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA D 246

Chain	Residue
D	SER136
D	LEU146
D	TYR149
D	NDP245

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. SmvahvtfpnLitYSSTKGAMtMLTkAMA

Chain	Residue	Details
A	SER136-ALA164

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	112
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8805511","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	SER136
A	TYR149
A	LYS153

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LEU146
B	LYS153

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LEU146
C	LYS153

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LEU146
D	LYS153

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	TYR149
A	LYS153

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	TYR149
B	LYS153

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	TYR149
C	LYS153

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	TYR149
D	LYS153

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	SER136
B	TYR149
B	LYS153

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	SER136
C	TYR149
C	LYS153

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	SER136
D	TYR149
D	LYS153

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	SER136
A	ASN107
A	TYR149
A	LYS153

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	SER136
B	ASN107
B	TYR149
B	LYS153

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	SER136
C	ASN107
C	TYR149
C	LYS153

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	SER136
D	ASN107
D	TYR149
D	LYS153

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LEU146
A	LYS153

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