Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Z9N

X-Ray structure of a Cu-Zn superoxide dismutase from Haemophilus ducreyi with haem bound at the dimer interface

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004784	molecular_function	superoxide dismutase activity
A	0005507	molecular_function	copper ion binding
A	0006801	biological_process	superoxide metabolic process
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0019430	biological_process	removal of superoxide radicals
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
B	0004784	molecular_function	superoxide dismutase activity
B	0005507	molecular_function	copper ion binding
B	0006801	biological_process	superoxide metabolic process
B	0016209	molecular_function	antioxidant activity
B	0016491	molecular_function	oxidoreductase activity
B	0019430	biological_process	removal of superoxide radicals
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0004784	molecular_function	superoxide dismutase activity
C	0005507	molecular_function	copper ion binding
C	0006801	biological_process	superoxide metabolic process
C	0016209	molecular_function	antioxidant activity
C	0016491	molecular_function	oxidoreductase activity
C	0019430	biological_process	removal of superoxide radicals
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
D	0004784	molecular_function	superoxide dismutase activity
D	0005507	molecular_function	copper ion binding
D	0006801	biological_process	superoxide metabolic process
D	0016209	molecular_function	antioxidant activity
D	0016491	molecular_function	oxidoreductase activity
D	0019430	biological_process	removal of superoxide radicals
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 200

Chain	Residue
A	HIS70
A	HIS72
A	HIS95
A	HIS151

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 201

Chain	Residue
A	HIS95
A	HIS104
A	HIS113
A	ASP116

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 200

Chain	Residue
B	HIS72
B	HIS95
B	HIS151
B	HIS70

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 201

Chain	Residue
B	HIS95
B	HIS104
B	HIS113
B	ASP116

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 200

Chain	Residue
C	HIS70
C	HIS72
C	HIS95
C	HIS151

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 201

Chain	Residue
C	HIS95
C	HIS104
C	HIS113
C	ASP116

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU D 200

Chain	Residue
D	HIS70
D	HIS72
D	HIS95
D	HIS151
D	HOH319

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 201

Chain	Residue
D	HIS95
D	HIS104
D	HIS113
D	ASP116

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM A 1001

Chain	Residue
A	HIS64
A	PHE121
A	HIS124
A	HOH1055
A	HOH1086
A	HOH1165
A	HOH1182
A	HOH1206
B	HIS64
B	GLY65
B	VAL122
B	MET123
B	HIS124
C	GLU23
D	GLU48
D	SER49
D	ALA50

site_id	BC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM C 2001

Chain	Residue
A	GLU48
A	SER49
A	ALA50
B	GLU23
C	HIS64
C	GLY65
C	VAL122
C	MET123
C	HIS124
C	HOH2052
C	HOH2143
C	HOH2152
C	HOH2165
C	HOH2221
C	HOH2235
C	HOH2265
C	HOH2279
D	HIS64
D	PHE121
D	HIS124

Functional Information from PROSITE/UniProt

site_id	PS00087
Number of Residues	11
Details	SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHEkPScE

Chain	Residue	Details
A	GLY68-GLU78

site_id	PS00332
Number of Residues	12
Details	SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GGGGpRmACgvI

Chain	Residue	Details
A	GLY165-ILE176

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	HIS70
B	HIS95
B	HIS104
B	HIS113
B	ASP116
B	HIS151
C	HIS70
C	HIS72
C	HIS95
C	HIS104
C	HIS113
A	HIS72
C	ASP116
C	HIS151
D	HIS70
D	HIS72
D	HIS95
D	HIS104
D	HIS113
D	ASP116
D	HIS151
A	HIS95
A	HIS104
A	HIS113
A	ASP116
A	HIS151
B	HIS70
B	HIS72

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
A	ARG170
A	HIS95

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
B	ARG170
B	HIS95

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
C	ARG170
C	HIS95

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
D	ARG170
D	HIS95

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
A	HIS95

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
B	HIS95

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
C	HIS95

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
D	HIS95

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