Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CTM

Crystal Structure of a Carbonyl Reductase from Candida Parapsilosis with anti-Prelog Stereo-specificity

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003674	molecular_function	molecular_function
A	0004090	molecular_function	carbonyl reductase (NADPH) activity
A	0005575	cellular_component	cellular_component
A	0005975	biological_process	carbohydrate metabolic process
A	0008150	biological_process	biological_process
A	0016491	molecular_function	oxidoreductase activity
A	0044281	biological_process	small molecule metabolic process
A	0046872	molecular_function	metal ion binding
A	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
A	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
B	0000166	molecular_function	nucleotide binding
B	0003674	molecular_function	molecular_function
B	0004090	molecular_function	carbonyl reductase (NADPH) activity
B	0005575	cellular_component	cellular_component
B	0005975	biological_process	carbohydrate metabolic process
B	0008150	biological_process	biological_process
B	0016491	molecular_function	oxidoreductase activity
B	0044281	biological_process	small molecule metabolic process
B	0046872	molecular_function	metal ion binding
B	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
B	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
C	0000166	molecular_function	nucleotide binding
C	0003674	molecular_function	molecular_function
C	0004090	molecular_function	carbonyl reductase (NADPH) activity
C	0005575	cellular_component	cellular_component
C	0005975	biological_process	carbohydrate metabolic process
C	0008150	biological_process	biological_process
C	0016491	molecular_function	oxidoreductase activity
C	0044281	biological_process	small molecule metabolic process
C	0046872	molecular_function	metal ion binding
C	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
C	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
D	0000166	molecular_function	nucleotide binding
D	0003674	molecular_function	molecular_function
D	0004090	molecular_function	carbonyl reductase (NADPH) activity
D	0005575	cellular_component	cellular_component
D	0005975	biological_process	carbohydrate metabolic process
D	0008150	biological_process	biological_process
D	0016491	molecular_function	oxidoreductase activity
D	0044281	biological_process	small molecule metabolic process
D	0046872	molecular_function	metal ion binding
D	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
D	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
E	0000166	molecular_function	nucleotide binding
E	0003674	molecular_function	molecular_function
E	0004090	molecular_function	carbonyl reductase (NADPH) activity
E	0005575	cellular_component	cellular_component
E	0005975	biological_process	carbohydrate metabolic process
E	0008150	biological_process	biological_process
E	0016491	molecular_function	oxidoreductase activity
E	0044281	biological_process	small molecule metabolic process
E	0046872	molecular_function	metal ion binding
E	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
E	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
F	0000166	molecular_function	nucleotide binding
F	0003674	molecular_function	molecular_function
F	0004090	molecular_function	carbonyl reductase (NADPH) activity
F	0005575	cellular_component	cellular_component
F	0005975	biological_process	carbohydrate metabolic process
F	0008150	biological_process	biological_process
F	0016491	molecular_function	oxidoreductase activity
F	0044281	biological_process	small molecule metabolic process
F	0046872	molecular_function	metal ion binding
F	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
F	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
G	0000166	molecular_function	nucleotide binding
G	0003674	molecular_function	molecular_function
G	0004090	molecular_function	carbonyl reductase (NADPH) activity
G	0005575	cellular_component	cellular_component
G	0005975	biological_process	carbohydrate metabolic process
G	0008150	biological_process	biological_process
G	0016491	molecular_function	oxidoreductase activity
G	0044281	biological_process	small molecule metabolic process
G	0046872	molecular_function	metal ion binding
G	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
G	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
H	0000166	molecular_function	nucleotide binding
H	0003674	molecular_function	molecular_function
H	0004090	molecular_function	carbonyl reductase (NADPH) activity
H	0005575	cellular_component	cellular_component
H	0005975	biological_process	carbohydrate metabolic process
H	0008150	biological_process	biological_process
H	0016491	molecular_function	oxidoreductase activity
H	0044281	biological_process	small molecule metabolic process
H	0046872	molecular_function	metal ion binding
H	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
H	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor

Catalytic Information from CSA

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

Chain	Residue	Details
A	TYR187
A	LYS191
A	SER171

site_id	CSA10
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	TYR187
B	SER172
B	ASP144
B	LYS191

site_id	CSA11
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	TYR187
C	SER172
C	ASP144
C	LYS191

site_id	CSA12
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	TYR187
D	SER172
D	ASP144
D	LYS191

site_id	CSA13
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
E	TYR187
E	SER172
E	ASP144
E	LYS191

site_id	CSA14
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
F	TYR187
F	SER172
F	ASP144
F	LYS191

site_id	CSA15
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
G	TYR187
G	SER172
G	ASP144
G	LYS191

site_id	CSA16
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
H	TYR187
H	SER172
H	ASP144
H	LYS191

site_id	CSA17
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	TYR187
A	LYS191

site_id	CSA18
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	TYR187
B	LYS191

site_id	CSA19
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	TYR187
C	LYS191

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

Chain	Residue	Details
B	TYR187
B	LYS191
B	SER171

site_id	CSA20
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	TYR187
D	LYS191

site_id	CSA21
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
E	TYR187
E	LYS191

site_id	CSA22
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
F	TYR187
F	LYS191

site_id	CSA23
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
G	TYR187
G	LYS191

site_id	CSA24
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
H	TYR187
H	LYS191

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

Chain	Residue	Details
C	TYR187
C	LYS191
C	SER171

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

Chain	Residue	Details
D	TYR187
D	LYS191
D	SER171

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
E	TYR187
E	LYS191
E	SER171

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
F	TYR187
F	LYS191
F	SER171

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
G	TYR187
G	LYS191
G	SER171

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
H	TYR187
H	LYS191
H	SER171

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	TYR187
A	SER172
A	ASP144
A	LYS191

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