Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SI4

Crystal structure of Human hemoglobin A2 (in R2 state) at 2.2 A resolution

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN A 143

Chain	Residue
A	LEU29
A	HIS58
A	VAL62
A	HEM142

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN B 148

Chain	Residue
B	LEU28
B	PHE42
B	HIS63
B	VAL67
B	HEM147

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN C 143

Chain	Residue
C	LEU29
C	HIS58
C	VAL62
C	HEM142

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN D 148

Chain	Residue
D	LEU28
D	PHE42
D	HIS63
D	VAL67
D	HEM147

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 142

Chain	Residue
A	TYR42
A	PHE43
A	PHE46
A	HIS58
A	VAL62
A	ALA65
A	LEU83
A	LEU86
A	HIS87
A	ASN97
A	PHE98
A	LEU101
A	VAL132
A	CYN143
C	HIS45

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM B 147

Chain	Residue
A	ARG141
B	THR38
B	PHE41
B	PHE42
B	HIS63
B	LYS66
B	ALA70
B	PHE71
B	LEU91
B	HIS92
B	VAL98
B	ASN102
B	PHE103
B	LEU106
B	CYN148
B	HOH1016
B	HOH1120
B	HOH1580

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM C 142

Chain	Residue
C	TYR42
C	PHE43
C	PHE46
C	HIS58
C	LEU86
C	HIS87
C	LEU91
C	VAL93
C	ASN97
C	PHE98
C	CYN143
C	HOH1296
D	LYS120
D	HOH1520

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM D 147

Chain	Residue
D	PHE41
D	PHE42
D	HIS63
D	ALA70
D	LEU88
D	HIS92
D	LEU96
D	VAL98
D	ASN102
D	LEU106
D	LEU141
D	CYN148
D	HOH1337
D	HOH1402
D	HOH1489
D	HOH1634

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	568
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	8
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":"15449937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SHR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SI4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine; in variant Niigata","evidences":[{"source":"PubMed","id":"1787103","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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