Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XDQ

Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
A	0016667	molecular_function	oxidoreductase activity, acting on a sulfur group of donors
A	0016672	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
A	0016675	molecular_function	oxidoreductase activity, acting on a heme group of donors
A	0030091	biological_process	protein repair
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0043546	molecular_function	molybdopterin cofactor binding
A	0046872	molecular_function	metal ion binding
A	0055114	biological_process	obsolete oxidation-reduction process
A	1901530	biological_process	response to hypochlorite
B	0016491	molecular_function	oxidoreductase activity
B	0016667	molecular_function	oxidoreductase activity, acting on a sulfur group of donors
B	0016672	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
B	0016675	molecular_function	oxidoreductase activity, acting on a heme group of donors
B	0030091	biological_process	protein repair
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0043546	molecular_function	molybdopterin cofactor binding
B	0046872	molecular_function	metal ion binding
B	0055114	biological_process	obsolete oxidation-reduction process
B	1901530	biological_process	response to hypochlorite
C	0016491	molecular_function	oxidoreductase activity
C	0016667	molecular_function	oxidoreductase activity, acting on a sulfur group of donors
C	0016672	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
C	0016675	molecular_function	oxidoreductase activity, acting on a heme group of donors
C	0030091	biological_process	protein repair
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0043546	molecular_function	molybdopterin cofactor binding
C	0046872	molecular_function	metal ion binding
C	0055114	biological_process	obsolete oxidation-reduction process
C	1901530	biological_process	response to hypochlorite
D	0016491	molecular_function	oxidoreductase activity
D	0016667	molecular_function	oxidoreductase activity, acting on a sulfur group of donors
D	0016672	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
D	0016675	molecular_function	oxidoreductase activity, acting on a heme group of donors
D	0030091	biological_process	protein repair
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0043546	molecular_function	molybdopterin cofactor binding
D	0046872	molecular_function	metal ion binding
D	0055114	biological_process	obsolete oxidation-reduction process
D	1901530	biological_process	response to hypochlorite
E	0016491	molecular_function	oxidoreductase activity
E	0016667	molecular_function	oxidoreductase activity, acting on a sulfur group of donors
E	0016672	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
E	0016675	molecular_function	oxidoreductase activity, acting on a heme group of donors
E	0030091	biological_process	protein repair
E	0030288	cellular_component	outer membrane-bounded periplasmic space
E	0042597	cellular_component	periplasmic space
E	0043546	molecular_function	molybdopterin cofactor binding
E	0046872	molecular_function	metal ion binding
E	0055114	biological_process	obsolete oxidation-reduction process
E	1901530	biological_process	response to hypochlorite

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE URE A 401

Chain	Residue
A	TYR47
A	GLU104
A	TRP223
A	TYR231

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE URE B 402

Chain	Residue
B	HOH628
B	TYR47
B	GLU104
B	TRP223
B	TYR231
B	ARG245

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE URE C 403

Chain	Residue
C	TYR47
C	GLU104
C	TRP223
C	TYR231
C	ARG245

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE URE D 404

Chain	Residue
D	TYR47
D	GLU104
D	TRP223
D	TYR231
D	ARG245
D	HOH629

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE URE E 405

Chain	Residue
E	TYR47
E	GLU104
E	TRP223
E	TYR231
E	HOH630

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MO A 501

Chain	Residue
A	ASN45
A	CYS102
A	MTE301
A	O601
A	HOH645

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MO B 502

Chain	Residue
B	ASN45
B	CYS102
B	MTE302
B	O602
B	HOH628

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MO C 503

Chain	Residue
C	CYS102
C	MTE303
C	O603
C	HOH621

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MO D 504

Chain	Residue
D	CYS102
D	MTE304
D	O604
D	HOH629

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MO E 505

Chain	Residue
E	ASN45
E	CYS102
E	MTE305
E	O605
E	HOH630

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE O A 601

Chain	Residue
A	CYS102
A	VAL103
A	GLY202
A	PHE203
A	MTE301
A	MO501

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE O B 602

Chain	Residue
B	CYS102
B	VAL103
B	GLY202
B	PHE203
B	MTE302
B	MO502

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE O C 603

Chain	Residue
C	CYS102
C	VAL103
C	GLY202
C	PHE203
C	MTE303
C	MO503
C	HOH621

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE O D 604

Chain	Residue
D	CYS102
D	VAL103
D	GLY202
D	PHE203
D	MTE304
D	MO504

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE O E 605

Chain	Residue
E	CYS102
E	VAL103
E	GLY202
E	PHE203
E	MTE305
E	MO505

site_id	BC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTE A 301

Chain	Residue
A	ASN44
A	ASN45
A	PHE46
A	TYR47
A	GLU48
A	CYS102
A	MET108
A	THR137
A	TYR160
A	ASN189
A	ARG194
A	GLY202
A	GLY205
A	LYS207
A	MO501
A	O601
A	HOH645

site_id	BC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTE B 302

Chain	Residue
B	PHE46
B	TYR47
B	GLU48
B	CYS102
B	MET108
B	THR137
B	TYR160
B	ASN189
B	ARG194
B	GLY202
B	PHE203
B	GLY205
B	LYS207
B	MO502
B	O602
B	ASN44
B	ASN45

site_id	BC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTE C 303

Chain	Residue
C	ASN44
C	ASN45
C	PHE46
C	TYR47
C	GLU48
C	CYS102
C	MET108
C	THR137
C	TYR160
C	ASN189
C	ARG194
C	GLY202
C	PHE203
C	GLY205
C	LYS207
C	MO503
C	O603
C	HOH621

site_id	CC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTE D 304

Chain	Residue
D	ASN44
D	ASN45
D	PHE46
D	TYR47
D	GLU48
D	CYS102
D	MET108
D	THR137
D	TYR160
D	ASN189
D	ARG194
D	GLY202
D	PHE203
D	GLY205
D	LYS207
D	MO504
D	O604
D	HOH629

site_id	CC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTE E 305

Chain	Residue
E	ASN44
E	ASN45
E	PHE46
E	TYR47
E	GLU48
E	CYS102
E	MET108
E	THR137
E	TYR160
E	ASN189
E	ARG194
E	GLY202
E	PHE203
E	GLY205
E	LYS207
E	MO505
E	O605
E	HOH630

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15355966","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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