Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Z3B

Crystal Structure of Bacillus Subtilis CodW, a non-canonical HslV-like peptidase with an impaired catalytic apparatus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000502	cellular_component	proteasome complex
A	0004298	molecular_function	threonine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0005839	cellular_component	proteasome core complex
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0009376	cellular_component	HslUV protease complex
A	0016787	molecular_function	hydrolase activity
A	0030163	biological_process	protein catabolic process
A	0046872	molecular_function	metal ion binding
A	0051603	biological_process	proteolysis involved in protein catabolic process
B	0000502	cellular_component	proteasome complex
B	0004298	molecular_function	threonine-type endopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0005839	cellular_component	proteasome core complex
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0009376	cellular_component	HslUV protease complex
B	0016787	molecular_function	hydrolase activity
B	0030163	biological_process	protein catabolic process
B	0046872	molecular_function	metal ion binding
B	0051603	biological_process	proteolysis involved in protein catabolic process
C	0000502	cellular_component	proteasome complex
C	0004298	molecular_function	threonine-type endopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0005839	cellular_component	proteasome core complex
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008236	molecular_function	serine-type peptidase activity
C	0009376	cellular_component	HslUV protease complex
C	0016787	molecular_function	hydrolase activity
C	0030163	biological_process	protein catabolic process
C	0046872	molecular_function	metal ion binding
C	0051603	biological_process	proteolysis involved in protein catabolic process
D	0000502	cellular_component	proteasome complex
D	0004298	molecular_function	threonine-type endopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0005839	cellular_component	proteasome core complex
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0009376	cellular_component	HslUV protease complex
D	0016787	molecular_function	hydrolase activity
D	0030163	biological_process	protein catabolic process
D	0046872	molecular_function	metal ion binding
D	0051603	biological_process	proteolysis involved in protein catabolic process
E	0000502	cellular_component	proteasome complex
E	0004298	molecular_function	threonine-type endopeptidase activity
E	0005737	cellular_component	cytoplasm
E	0005839	cellular_component	proteasome core complex
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0008236	molecular_function	serine-type peptidase activity
E	0009376	cellular_component	HslUV protease complex
E	0016787	molecular_function	hydrolase activity
E	0030163	biological_process	protein catabolic process
E	0046872	molecular_function	metal ion binding
E	0051603	biological_process	proteolysis involved in protein catabolic process
F	0000502	cellular_component	proteasome complex
F	0004298	molecular_function	threonine-type endopeptidase activity
F	0005737	cellular_component	cytoplasm
F	0005839	cellular_component	proteasome core complex
F	0006508	biological_process	proteolysis
F	0008233	molecular_function	peptidase activity
F	0008236	molecular_function	serine-type peptidase activity
F	0009376	cellular_component	HslUV protease complex
F	0016787	molecular_function	hydrolase activity
F	0030163	biological_process	protein catabolic process
F	0046872	molecular_function	metal ion binding
F	0051603	biological_process	proteolysis involved in protein catabolic process
G	0000502	cellular_component	proteasome complex
G	0004298	molecular_function	threonine-type endopeptidase activity
G	0005737	cellular_component	cytoplasm
G	0005839	cellular_component	proteasome core complex
G	0006508	biological_process	proteolysis
G	0008233	molecular_function	peptidase activity
G	0008236	molecular_function	serine-type peptidase activity
G	0009376	cellular_component	HslUV protease complex
G	0016787	molecular_function	hydrolase activity
G	0030163	biological_process	protein catabolic process
G	0046872	molecular_function	metal ion binding
G	0051603	biological_process	proteolysis involved in protein catabolic process
H	0000502	cellular_component	proteasome complex
H	0004298	molecular_function	threonine-type endopeptidase activity
H	0005737	cellular_component	cytoplasm
H	0005839	cellular_component	proteasome core complex
H	0006508	biological_process	proteolysis
H	0008233	molecular_function	peptidase activity
H	0008236	molecular_function	serine-type peptidase activity
H	0009376	cellular_component	HslUV protease complex
H	0016787	molecular_function	hydrolase activity
H	0030163	biological_process	protein catabolic process
H	0046872	molecular_function	metal ion binding
H	0051603	biological_process	proteolysis involved in protein catabolic process
I	0000502	cellular_component	proteasome complex
I	0004298	molecular_function	threonine-type endopeptidase activity
I	0005737	cellular_component	cytoplasm
I	0005839	cellular_component	proteasome core complex
I	0006508	biological_process	proteolysis
I	0008233	molecular_function	peptidase activity
I	0008236	molecular_function	serine-type peptidase activity
I	0009376	cellular_component	HslUV protease complex
I	0016787	molecular_function	hydrolase activity
I	0030163	biological_process	protein catabolic process
I	0046872	molecular_function	metal ion binding
I	0051603	biological_process	proteolysis involved in protein catabolic process
J	0000502	cellular_component	proteasome complex
J	0004298	molecular_function	threonine-type endopeptidase activity
J	0005737	cellular_component	cytoplasm
J	0005839	cellular_component	proteasome core complex
J	0006508	biological_process	proteolysis
J	0008233	molecular_function	peptidase activity
J	0008236	molecular_function	serine-type peptidase activity
J	0009376	cellular_component	HslUV protease complex
J	0016787	molecular_function	hydrolase activity
J	0030163	biological_process	protein catabolic process
J	0046872	molecular_function	metal ion binding
J	0051603	biological_process	proteolysis involved in protein catabolic process
K	0000502	cellular_component	proteasome complex
K	0004298	molecular_function	threonine-type endopeptidase activity
K	0005737	cellular_component	cytoplasm
K	0005839	cellular_component	proteasome core complex
K	0006508	biological_process	proteolysis
K	0008233	molecular_function	peptidase activity
K	0008236	molecular_function	serine-type peptidase activity
K	0009376	cellular_component	HslUV protease complex
K	0016787	molecular_function	hydrolase activity
K	0030163	biological_process	protein catabolic process
K	0046872	molecular_function	metal ion binding
K	0051603	biological_process	proteolysis involved in protein catabolic process
L	0000502	cellular_component	proteasome complex
L	0004298	molecular_function	threonine-type endopeptidase activity
L	0005737	cellular_component	cytoplasm
L	0005839	cellular_component	proteasome core complex
L	0006508	biological_process	proteolysis
L	0008233	molecular_function	peptidase activity
L	0008236	molecular_function	serine-type peptidase activity
L	0009376	cellular_component	HslUV protease complex
L	0016787	molecular_function	hydrolase activity
L	0030163	biological_process	protein catabolic process
L	0046872	molecular_function	metal ion binding
L	0051603	biological_process	proteolysis involved in protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 1001

Chain	Residue
A	GLY164
A	CYS167
A	THR170

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 1002

Chain	Residue
B	GLY164
B	CYS167
B	THR170
B	HOH1010

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 1003

Chain	Residue
C	THR170
C	HOH1024
C	GLY164
C	CYS167

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA D 1004

Chain	Residue
D	GLY164
D	CYS167
D	THR170

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA E 1005

Chain	Residue
E	GLY164
E	CYS167
E	THR170

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA F 1006

Chain	Residue
F	GLY164
F	CYS167
F	THR170

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA G 1007

Chain	Residue
G	GLY164
G	CYS167
G	THR170

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA J 1008

Chain	Residue
J	GLY164
J	CYS167
J	THR170

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA I 1009

Chain	Residue
I	GLY164
I	CYS167
I	THR170

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA H 1010

Chain	Residue
H	GLY164
H	CYS167

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA K 1011

Chain	Residue
K	GLY164
K	CYS167

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA L 1012

Chain	Residue
L	GLY164
L	CYS167
L	THR170

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
A	THR6
A	GLY54
A	LYS39
A	SER130

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

Chain	Residue	Details
J	THR6
J	GLY54
J	LYS39
J	SER130

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

Chain	Residue	Details
K	THR6
K	GLY54
K	LYS39
K	SER130

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

Chain	Residue	Details
L	THR6
L	GLY54
L	LYS39
L	SER130

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

Chain	Residue	Details
A	THR6
A	GLY51
A	LYS39
A	SER130

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

Chain	Residue	Details
B	THR6
B	GLY51
B	LYS39
B	SER130

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

Chain	Residue	Details
C	THR6
C	GLY51
C	LYS39
C	SER130

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

Chain	Residue	Details
D	THR6
D	GLY51
D	LYS39
D	SER130

site_id	CSA17
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
E	THR6
E	GLY51
E	LYS39
E	SER130

site_id	CSA18
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
F	THR6
F	GLY51
F	LYS39
F	SER130

site_id	CSA19
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
G	THR6
G	GLY51
G	LYS39
G	SER130

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
B	THR6
B	GLY54
B	LYS39
B	SER130

site_id	CSA20
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
H	THR6
H	GLY51
H	LYS39
H	SER130

site_id	CSA21
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
I	THR6
I	GLY51
I	LYS39
I	SER130

site_id	CSA22
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
J	THR6
J	GLY51
J	LYS39
J	SER130

site_id	CSA23
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
K	THR6
K	GLY51
K	LYS39
K	SER130

site_id	CSA24
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
L	THR6
L	GLY51
L	LYS39
L	SER130

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
C	THR6
C	GLY54
C	LYS39
C	SER130

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
D	THR6
D	GLY54
D	LYS39
D	SER130

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

Chain	Residue	Details
E	THR6
E	GLY54
E	LYS39
E	SER130

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

Chain	Residue	Details
F	THR6
F	GLY54
F	LYS39
F	SER130

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

Chain	Residue	Details
G	THR6
G	GLY54
G	LYS39
G	SER130

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

Chain	Residue	Details
H	THR6
H	GLY54
H	LYS39
H	SER130

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

Chain	Residue	Details
I	THR6
I	GLY54
I	LYS39
I	SER130

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