Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RT8

Structure of catharanthine synthase - an alpha-beta hydrolase from Catharanthus roseus with a cleaviminium intermediate bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009820	biological_process	alkaloid metabolic process
A	0009821	biological_process	alkaloid biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0016853	molecular_function	isomerase activity
A	0035834	biological_process	indole alkaloid metabolic process
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009820	biological_process	alkaloid metabolic process
B	0009821	biological_process	alkaloid biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0016853	molecular_function	isomerase activity
B	0035834	biological_process	indole alkaloid metabolic process
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009820	biological_process	alkaloid metabolic process
C	0009821	biological_process	alkaloid biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0016853	molecular_function	isomerase activity
C	0035834	biological_process	indole alkaloid metabolic process
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009820	biological_process	alkaloid metabolic process
D	0009821	biological_process	alkaloid biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0016853	molecular_function	isomerase activity
D	0035834	biological_process	indole alkaloid metabolic process
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0009820	biological_process	alkaloid metabolic process
E	0009821	biological_process	alkaloid biosynthetic process
E	0016787	molecular_function	hydrolase activity
E	0016853	molecular_function	isomerase activity
E	0035834	biological_process	indole alkaloid metabolic process
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009820	biological_process	alkaloid metabolic process
F	0009821	biological_process	alkaloid biosynthetic process
F	0016787	molecular_function	hydrolase activity
F	0016853	molecular_function	isomerase activity
F	0035834	biological_process	indole alkaloid metabolic process
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0009820	biological_process	alkaloid metabolic process
G	0009821	biological_process	alkaloid biosynthetic process
G	0016787	molecular_function	hydrolase activity
G	0016853	molecular_function	isomerase activity
G	0035834	biological_process	indole alkaloid metabolic process
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0009820	biological_process	alkaloid metabolic process
H	0009821	biological_process	alkaloid biosynthetic process
H	0016787	molecular_function	hydrolase activity
H	0016853	molecular_function	isomerase activity
H	0035834	biological_process	indole alkaloid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue KJE A 401

Chain	Residue
A	TYR18
A	ILE268
A	TYR304
A	HIS31
A	ALA82
A	GLY83
A	SER172
A	PRO173
A	TYR205
A	ASN221
A	TYR225

site_id	AC2
Number of Residues	14
Details	binding site for residue P6G A 402

Chain	Residue
A	ASN32
A	TYR35
A	SER88
A	ARG91
A	GLU113
A	HOH552
A	HOH556
B	ARG29
B	ASN32
B	TYR35
B	SER88
B	ARG91
B	GLU113
B	LEU116

site_id	AC3
Number of Residues	10
Details	binding site for residue KJE B 401

Chain	Residue
B	TYR18
B	ALA82
B	GLY83
B	SER172
B	PRO173
B	TYR205
B	ASN221
B	TYR225
B	ILE268
B	TYR304

site_id	AC4
Number of Residues	12
Details	binding site for residue KJE C 401

Chain	Residue
C	TYR18
C	HIS31
C	ALA82
C	GLY83
C	SER172
C	PRO173
C	TYR205
C	PHE218
C	ASN221
C	TYR225
C	ILE268
C	TYR304

site_id	AC5
Number of Residues	9
Details	binding site for residue P6G C 402

Chain	Residue
C	ASN32
C	TYR35
C	SER88
C	ARG91
C	GLU113
D	ARG29
D	ASN32
D	TYR35
D	ARG91

site_id	AC6
Number of Residues	13
Details	binding site for residue KJE D 401

Chain	Residue
D	TYR18
D	HIS31
D	ALA82
D	GLY83
D	PHE93
D	SER172
D	PRO173
D	TYR203
D	TYR205
D	ASN221
D	TYR225
D	ILE268
D	TYR304

site_id	AC7
Number of Residues	11
Details	binding site for residue KJE E 401

Chain	Residue
E	TYR18
E	ALA82
E	GLY83
E	SER172
E	PRO173
E	TYR203
E	TYR205
E	ASN221
E	TYR225
E	ILE268
E	TYR304

site_id	AC8
Number of Residues	11
Details	binding site for residue P6G E 402

Chain	Residue
E	ASN32
E	TYR35
E	GLU87
E	SER88
E	ARG91
E	GLU113
F	ASN32
F	TYR35
F	SER88
F	ARG91
F	GLU113

site_id	AC9
Number of Residues	12
Details	binding site for residue KJE F 401

Chain	Residue
F	ASN221
F	TYR225
F	ILE268
F	TYR304
F	TYR18
F	HIS31
F	ALA82
F	GLY83
F	SER172
F	PRO173
F	TYR205
F	PHE218

site_id	AD1
Number of Residues	12
Details	binding site for residue KJE G 401

Chain	Residue
G	TYR18
G	HIS31
G	ALA82
G	GLY83
G	PHE93
G	SER172
G	PRO173
G	TYR205
G	ASN221
G	TYR225
G	ILE268
G	TYR304

site_id	AD2
Number of Residues	10
Details	binding site for residue KJE H 401

Chain	Residue
H	TYR18
H	ALA82
H	GLY83
H	PHE93
H	SER172
H	PRO173
H	TYR205
H	ASN221
H	TYR225
H	TYR304

site_id	AD3
Number of Residues	13
Details	binding site for residue P6G H 402

Chain	Residue
G	ARG29
G	ASN32
G	TYR35
G	SER88
G	ARG91
H	ARG29
H	ASN32
H	TYR35
H	GLU87
H	SER88
H	ARG91
H	GLU113
H	LEU116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:Q5NUF3

Chain	Residue	Details
A	SER172
E	ASP273
F	SER172
F	ASP273
G	SER172
G	ASP273
H	SER172
H	ASP273
A	ASP273
B	SER172
B	ASP273
C	SER172
C	ASP273
D	SER172
D	ASP273
E	SER172

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