Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HF4

Crystal structure of rat methemoglobin in R2 state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001540	molecular_function	amyloid-beta binding
A	0001664	molecular_function	G protein-coupled receptor binding
A	0004601	molecular_function	peroxidase activity
A	0005344	molecular_function	oxygen carrier activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005833	cellular_component	hemoglobin complex
A	0006954	biological_process	inflammatory response
A	0015670	biological_process	carbon dioxide transport
A	0015671	biological_process	oxygen transport
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0030185	biological_process	nitric oxide transport
A	0031720	molecular_function	haptoglobin binding
A	0031838	cellular_component	haptoglobin-hemoglobin complex
A	0032355	biological_process	response to estradiol
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0045776	biological_process	negative regulation of blood pressure
A	0046872	molecular_function	metal ion binding
A	0048821	biological_process	erythrocyte development
A	0098869	biological_process	cellular oxidant detoxification
B	0004601	molecular_function	peroxidase activity
B	0005344	molecular_function	oxygen carrier activity
B	0005615	cellular_component	extracellular space
B	0005833	cellular_component	hemoglobin complex
B	0006749	biological_process	glutathione metabolic process
B	0006954	biological_process	inflammatory response
B	0010999	biological_process	regulation of eIF2 alpha phosphorylation by heme
B	0015670	biological_process	carbon dioxide transport
B	0015671	biological_process	oxygen transport
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0030097	biological_process	hemopoiesis
B	0030185	biological_process	nitric oxide transport
B	0030492	molecular_function	hemoglobin binding
B	0031720	molecular_function	haptoglobin binding
B	0031721	molecular_function	hemoglobin alpha binding
B	0031722	molecular_function	hemoglobin beta binding
B	0031838	cellular_component	haptoglobin-hemoglobin complex
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0044877	molecular_function	protein-containing complex binding
B	0046872	molecular_function	metal ion binding
B	0048821	biological_process	erythrocyte development
B	0070293	biological_process	renal absorption
B	0098869	biological_process	cellular oxidant detoxification
E	0001540	molecular_function	amyloid-beta binding
E	0001664	molecular_function	G protein-coupled receptor binding
E	0004601	molecular_function	peroxidase activity
E	0005344	molecular_function	oxygen carrier activity
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0005615	cellular_component	extracellular space
E	0005833	cellular_component	hemoglobin complex
E	0006954	biological_process	inflammatory response
E	0015670	biological_process	carbon dioxide transport
E	0015671	biological_process	oxygen transport
E	0019825	molecular_function	oxygen binding
E	0020037	molecular_function	heme binding
E	0030185	biological_process	nitric oxide transport
E	0031720	molecular_function	haptoglobin binding
E	0031838	cellular_component	haptoglobin-hemoglobin complex
E	0032355	biological_process	response to estradiol
E	0042542	biological_process	response to hydrogen peroxide
E	0042744	biological_process	hydrogen peroxide catabolic process
E	0045776	biological_process	negative regulation of blood pressure
E	0046872	molecular_function	metal ion binding
E	0048821	biological_process	erythrocyte development
E	0098869	biological_process	cellular oxidant detoxification
F	0004601	molecular_function	peroxidase activity
F	0005344	molecular_function	oxygen carrier activity
F	0005615	cellular_component	extracellular space
F	0005833	cellular_component	hemoglobin complex
F	0006749	biological_process	glutathione metabolic process
F	0006954	biological_process	inflammatory response
F	0010999	biological_process	regulation of eIF2 alpha phosphorylation by heme
F	0015670	biological_process	carbon dioxide transport
F	0015671	biological_process	oxygen transport
F	0019825	molecular_function	oxygen binding
F	0020037	molecular_function	heme binding
F	0030097	biological_process	hemopoiesis
F	0030185	biological_process	nitric oxide transport
F	0030492	molecular_function	hemoglobin binding
F	0031720	molecular_function	haptoglobin binding
F	0031721	molecular_function	hemoglobin alpha binding
F	0031722	molecular_function	hemoglobin beta binding
F	0031838	cellular_component	haptoglobin-hemoglobin complex
F	0042542	biological_process	response to hydrogen peroxide
F	0042744	biological_process	hydrogen peroxide catabolic process
F	0044877	molecular_function	protein-containing complex binding
F	0046872	molecular_function	metal ion binding
F	0048821	biological_process	erythrocyte development
F	0070293	biological_process	renal absorption
F	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 142

Chain	Residue
A	TYR42
A	VAL93
A	ASN97
A	PHE98
A	LEU101
A	VAL132
A	HOH144
A	PHE43
A	HIS45
A	HIS58
A	LYS61
A	LEU83
A	LEU86
A	HIS87
A	LEU91

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM B 147

Chain	Residue
B	TYR41
B	PHE42
B	HIS63
B	LYS66
B	VAL67
B	LEU88
B	HIS92
B	VAL98
B	ASN102
B	LEU106
B	LEU141
B	HOH149

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM E 142

Chain	Residue
E	TYR42
E	PHE43
E	HIS45
E	HIS58
E	LYS61
E	LEU86
E	HIS87
E	LEU91
E	VAL93
E	ASN97
E	PHE98
E	LEU101
E	HOH143

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM F 147

Chain	Residue
F	TYR41
F	PHE42
F	HIS63
F	LYS66
F	VAL67
F	LEU88
F	HIS92
F	LEU96
F	VAL98
F	ASN102
F	PHE103
F	LEU106
F	LEU141

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Peptide: {"description":"Hemopressin","featureId":"PRO_0000455938","evidences":[{"source":"PubMed","id":"12500972","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	424
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Binding site: {"description":"distal binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Binding site: {"description":"proximal binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N-acetylvaline","evidences":[{"source":"UniProtKB","id":"P02086","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02088","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P11517","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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