Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SZO

Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase His122Ala Mutant Bound to Its Natural Product (2S,4S)-alpha-Campholinic Acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
B	0016787	molecular_function	hydrolase activity
B	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
C	0016787	molecular_function	hydrolase activity
C	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
D	0016787	molecular_function	hydrolase activity
D	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
E	0016787	molecular_function	hydrolase activity
E	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
F	0016787	molecular_function	hydrolase activity
F	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
G	0016787	molecular_function	hydrolase activity
G	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
H	0016787	molecular_function	hydrolase activity
H	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
I	0016787	molecular_function	hydrolase activity
I	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
J	0016787	molecular_function	hydrolase activity
J	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
K	0016787	molecular_function	hydrolase activity
K	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
L	0016787	molecular_function	hydrolase activity
L	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 2001

Chain	Residue
A	HOH5058
A	HOH5059
B	ASP186
B	HOH5092
B	HOH5108
C	HOH5039
C	HOH5077

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA F 2002

Chain	Residue
E	HOH5074
E	HOH5152
F	ASP186
F	HOH5112
F	HOH5132
D	HOH5090
E	HOH5022

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA I 2003

Chain	Residue
G	HOH5045
G	HOH5129
H	HOH5116
I	HOH5057
I	HOH5066
I	HOH5069

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA K 2004

Chain	Residue
J	HOH5051
J	HOH5102
J	HOH5111
K	HOH5065
K	HOH5066
L	HOH5143

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX A 5001

Chain	Residue
A	TRP40
A	HIS45
A	ILE77
A	PHE82
A	ILE93
A	HIS145
A	ASP154
A	GLU244
A	HOH5007

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CAX B 5002

Chain	Residue
B	TRP40
B	HIS45
B	ILE77
B	PHE82
B	HIS145
B	ASP154
B	GLU244
B	HOH5032

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX C 5003

Chain	Residue
C	TRP40
C	HIS45
C	ILE77
C	PHE82
C	ILE93
C	HIS145
C	ASP154
C	GLU244
C	HOH5034

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX D 5004

Chain	Residue
D	TRP40
D	HIS45
D	ILE77
D	PHE82
D	ILE93
D	HIS145
D	ASP154
D	GLU244
D	HOH5021

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX E 5005

Chain	Residue
E	TRP40
E	HIS45
E	ILE77
E	PHE82
E	ILE93
E	HIS145
E	ASP154
E	GLU244
E	HOH5036

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CAX F 5006

Chain	Residue
F	TRP40
F	HIS45
F	ILE77
F	PHE82
F	ILE93
F	HIS145
F	ASP154
F	GLU244
F	HOH5034
F	HOH5087

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX G 5007

Chain	Residue
G	TRP40
G	HIS45
G	ILE77
G	PHE82
G	ILE93
G	HIS145
G	ASP154
G	GLU244
G	HOH5052

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CAX H 5008

Chain	Residue
H	TRP40
H	HIS45
H	ILE77
H	PHE82
H	ILE93
H	HIS145
H	ASP154
H	GLU244
H	HOH5026
H	HOH5035

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX I 5009

Chain	Residue
I	TRP40
I	HIS45
I	ILE77
I	PHE82
I	ILE93
I	HIS145
I	ASP154
I	GLU244
I	HOH5027

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX J 5010

Chain	Residue
J	TRP40
J	HIS45
J	ILE77
J	PHE82
J	ILE93
J	HIS145
J	ASP154
J	GLU244
J	HOH5024

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX K 5011

Chain	Residue
K	TRP40
K	HIS45
K	ILE77
K	PHE82
K	ILE93
K	HIS145
K	ASP154
K	GLU244
K	HOH5044

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAX L 5012

Chain	Residue
L	TRP40
L	HIS45
L	ILE77
L	PHE82
L	ILE93
L	HIS145
L	ASP154
L	GLU244
L	HOH5066

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Nucleophile => ECO:0000250

Chain	Residue	Details
A	GLU124
J	GLU124
K	GLU124
L	GLU124
B	GLU124
C	GLU124
D	GLU124
E	GLU124
F	GLU124
G	GLU124
H	GLU124
I	GLU124

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:15138275

Chain	Residue	Details
A	TRP40
C	HIS145
C	ASP154
C	GLU244
D	TRP40
D	HIS145
D	ASP154
D	GLU244
E	TRP40
E	HIS145
E	ASP154
A	HIS145
E	GLU244
F	TRP40
F	HIS145
F	ASP154
F	GLU244
G	TRP40
G	HIS145
G	ASP154
G	GLU244
H	TRP40
A	ASP154
H	HIS145
H	ASP154
H	GLU244
I	TRP40
I	HIS145
I	ASP154
I	GLU244
J	TRP40
J	HIS145
J	ASP154
A	GLU244
J	GLU244
K	TRP40
K	HIS145
K	ASP154
K	GLU244
L	TRP40
L	HIS145
L	ASP154
L	GLU244
B	TRP40
B	HIS145
B	ASP154
B	GLU244
C	TRP40

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