Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FDH

STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005829	cellular_component	cytosol
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	0016020	cellular_component	membrane
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	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0048821	biological_process	erythrocyte development
A	0070062	cellular_component	extracellular exosome
A	0071682	cellular_component	endocytic vesicle lumen
A	0072562	cellular_component	blood microparticle
A	0098869	biological_process	cellular oxidant detoxification
B	0004601	molecular_function	peroxidase activity
B	0005344	molecular_function	oxygen carrier activity
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005829	cellular_component	cytosol
B	0005833	cellular_component	hemoglobin complex
B	0006954	biological_process	inflammatory response
B	0015670	biological_process	carbon dioxide transport
B	0015671	biological_process	oxygen transport
B	0016020	cellular_component	membrane
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0030185	biological_process	nitric oxide transport
B	0031720	molecular_function	haptoglobin 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	0046872	molecular_function	metal ion binding
B	0048821	biological_process	erythrocyte development
B	0070062	cellular_component	extracellular exosome
B	0071682	cellular_component	endocytic vesicle lumen
B	0072562	cellular_component	blood microparticle
B	0098869	biological_process	cellular oxidant detoxification
G	0005344	molecular_function	oxygen carrier activity
G	0005515	molecular_function	protein binding
G	0005829	cellular_component	cytosol
G	0005833	cellular_component	hemoglobin complex
G	0015670	biological_process	carbon dioxide transport
G	0015671	biological_process	oxygen transport
G	0019825	molecular_function	oxygen binding
G	0020037	molecular_function	heme binding
G	0031721	molecular_function	hemoglobin alpha binding
G	0031838	cellular_component	haptoglobin-hemoglobin complex
G	0046872	molecular_function	metal ion binding
G	0048821	biological_process	erythrocyte development
G	0072562	cellular_component	blood microparticle
H	0005344	molecular_function	oxygen carrier activity
H	0005515	molecular_function	protein binding
H	0005829	cellular_component	cytosol
H	0005833	cellular_component	hemoglobin complex
H	0015670	biological_process	carbon dioxide transport
H	0015671	biological_process	oxygen transport
H	0019825	molecular_function	oxygen binding
H	0020037	molecular_function	heme binding
H	0031721	molecular_function	hemoglobin alpha binding
H	0031838	cellular_component	haptoglobin-hemoglobin complex
H	0046872	molecular_function	metal ion binding
H	0048821	biological_process	erythrocyte development
H	0072562	cellular_component	blood microparticle

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	LEU91
A	VAL93
A	ASN97
A	PHE98
A	LEU101
A	LEU136
A	PHE43
A	HIS45
A	PHE46
A	HIS58
A	LYS61
A	LEU83
A	LEU86
A	HIS87

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

Chain	Residue
G	HIS63
G	VAL67
G	SER70
G	PHE85
G	LEU88
G	LEU91
G	HIS92
G	LEU96
G	ASN102
G	LEU106
G	LEU141
H	GLU5

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM B 142

Chain	Residue
B	TYR42
B	PHE43
B	HIS45
B	PHE46
B	HIS58
B	LYS61
B	LEU83
B	LEU86
B	HIS87
B	LEU91
B	VAL93
B	ASN97
B	PHE98
B	LEU101
B	LEU136

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM H 147

Chain	Residue
B	HIS72
H	HIS63
H	VAL67
H	SER70
H	PHE85
H	LEU88
H	LEU91
H	HIS92
H	LEU96
H	ASN102
H	LEU106
H	LEU141

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Peptide: {"description":"Hemopressin","featureId":"PRO_0000455882","evidences":[{"source":"PubMed","id":"18077343","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	280
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	28
Details	Site: {"description":"(Microbial infection) Cleavage; by N.americanus apr-2","evidences":[{"source":"PubMed","id":"12552433","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
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":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Binding site: {"description":"distal binding residue","evidences":[{"source":"UniProtKB","id":"P80044","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"881729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FDH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MQJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MQK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"N-acetylglycine; in form Hb F1","evidences":[{"source":"PubMed","id":"5554303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	10
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)