Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1WE1

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 in complex with heme

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004392	molecular_function	heme oxygenase (decyclizing) activity
A	0005886	cellular_component	plasma membrane
A	0006788	biological_process	heme oxidation
A	0006979	biological_process	response to oxidative stress
A	0015979	biological_process	photosynthesis
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042167	biological_process	heme catabolic process
A	0046872	molecular_function	metal ion binding
B	0004392	molecular_function	heme oxygenase (decyclizing) activity
B	0005886	cellular_component	plasma membrane
B	0006788	biological_process	heme oxidation
B	0006979	biological_process	response to oxidative stress
B	0015979	biological_process	photosynthesis
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0042167	biological_process	heme catabolic process
B	0046872	molecular_function	metal ion binding
C	0004392	molecular_function	heme oxygenase (decyclizing) activity
C	0005886	cellular_component	plasma membrane
C	0006788	biological_process	heme oxidation
C	0006979	biological_process	response to oxidative stress
C	0015979	biological_process	photosynthesis
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0042167	biological_process	heme catabolic process
C	0046872	molecular_function	metal ion binding
D	0004392	molecular_function	heme oxygenase (decyclizing) activity
D	0005886	cellular_component	plasma membrane
D	0006788	biological_process	heme oxidation
D	0006979	biological_process	response to oxidative stress
D	0015979	biological_process	photosynthesis
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0042167	biological_process	heme catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 241

Chain	Residue
A	LYS165
A	LYS168
D	LYS165
D	LYS168
D	ARG172

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 241

Chain	Residue
C	LYS168
C	ARG172
B	LYS165
B	LYS168
B	ARG172
C	LYS165

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 242

Chain	Residue
B	LYS14

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 241

Chain	Residue
C	ARG10

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 243

Chain	Residue
A	ARG108
A	ASP194

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 300

Chain	Residue
A	ARG10
A	HIS17
A	ALA20
A	LEU30
A	TYR125
A	THR126
A	GLY130
A	SER133
A	ILE137
A	LEU138
A	LYS168
A	ARG172
A	PHE203
A	HOH1006
D	LYS165

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM B 300

Chain	Residue
B	ARG10
B	HIS17
B	ALA20
B	VAL26
B	LEU30
B	TYR125
B	THR126
B	GLY130
B	SER133
B	GLY134
B	LEU138
B	PHE196
B	ASN199
B	HOH1007
B	HOH1051
C	LYS165

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM C 300

Chain	Residue
B	LYS165
C	ARG10
C	HIS17
C	ALA20
C	VAL26
C	TYR125
C	THR126
C	GLY130
C	SER133
C	ILE137
C	LEU138
C	PHE196
C	ASN199
C	HOH1008
C	HOH1011
C	HOH1012

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM D 300

Chain	Residue
A	LYS165
D	ARG10
D	HIS17
D	ALA20
D	VAL26
D	LEU30
D	TYR125
D	THR126
D	ARG127
D	GLY130
D	SER133
D	ILE137
D	ARG172
D	PHE196
D	ASN199
D	PHE203
D	HOH1009

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IPA D 1004

Chain	Residue
D	TYR156
D	PHE203

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IPA C 1003

Chain	Residue
C	TYR156
C	HOH1072

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IPA B 1002

Chain	Residue
B	PHE203

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IPA A 1001

Chain	Residue
A	PHE29
A	LEU42

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IPA A 1005

Chain	Residue
A	GLU54
A	MET57
A	ILE69
A	TYR70
A	PHE71
A	ASN75
A	TYR128

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IPA B 1006

Chain	Residue
B	TYR128
B	MET57
B	ILE69
B	TYR70
B	PHE71
B	LEU74
B	SER124

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPA C 1007

Chain	Residue
C	MET57
C	ILE69
C	PHE71
C	LEU74
C	ASN75
C	SER124

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IPA D 1008

Chain	Residue
D	MET57
D	ILE69
D	TYR70
D	PHE71
D	ASN75
D	SER124
D	TYR128

Functional Information from PROSITE/UniProt

site_id	PS00593
Number of Residues	11
Details	HEME_OXYGENASE Heme oxygenase signature. LVAHSYTRYLG

Chain	Residue	Details
A	LEU120-GLY130

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15560792","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WE1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"15560792","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WE1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1dve

Chain	Residue	Details
A	THR126
A	HIS17
A	ASP131
A	GLY134
A	ARG127
A	GLY130
A	TYR50

site_id	CSA2
Number of Residues	7
Details	Annotated By Reference To The Literature 1dve

Chain	Residue	Details
B	THR126
B	HIS17
B	ASP131
B	GLY134
B	ARG127
B	GLY130
B	TYR50

site_id	CSA3
Number of Residues	7
Details	Annotated By Reference To The Literature 1dve

Chain	Residue	Details
C	THR126
C	HIS17
C	ASP131
C	GLY134
C	ARG127
C	GLY130
C	TYR50

site_id	CSA4
Number of Residues	7
Details	Annotated By Reference To The Literature 1dve

Chain	Residue	Details
D	THR126
D	HIS17
D	ASP131
D	GLY134
D	ARG127
D	GLY130
D	TYR50

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

Chain	Residue	Details
A	GLY135
A	ASP131

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

Chain	Residue	Details
B	GLY135
B	ASP131

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

Chain	Residue	Details
C	GLY135
C	ASP131

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

Chain	Residue	Details
D	GLY135
D	ASP131

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