Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SHR

Crystal structure of ferrocyanide bound human hemoglobin A2 at 1.88A 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	4
Details	BINDING SITE FOR RESIDUE CYN B 348

Chain	Residue
B	LEU28
B	HIS63
B	VAL67
B	HEM347

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN C 543

Chain	Residue
C	HIS58
C	VAL62
C	HEM542
C	LEU29

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN D 748

Chain	Residue
D	LEU28
D	PHE42
D	HIS63
D	VAL67
D	HEM747

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 801

Chain	Residue
B	HIS143
B	HIS146
B	CYN809
D	HIS146

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FE D 802

Chain	Residue
D	HIS143
D	CYN808

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 803

Chain	Residue
A	ASP75
A	MET76
A	PRO77
A	HOH1143
A	HOH1248

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CYN B 804

Chain	Residue
B	LYS82
B	HIS143
B	CYN809
D	CYN805
D	CYN806
D	CYN807

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CYN D 805

Chain	Residue
B	CYN804
B	CYN809
D	LYS82
D	CYN806
D	CYN808
D	HOH1430
D	HOH1736

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN D 806

Chain	Residue
B	CYN804
D	CYN805
D	CYN807
D	CYN808

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CYN D 807

Chain	Residue
B	CYN804
B	CYN809
D	TYR145
D	HIS146
D	CYN806
D	CYN808

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CYN D 808

Chain	Residue
B	CYN809
D	LYS82
D	HIS143
D	FE802
D	CYN805
D	CYN806
D	CYN807

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CYN B 809

Chain	Residue
B	HIS143
B	HIS146
B	FE801
B	CYN804
D	LYS82
D	HIS146
D	CYN805
D	CYN807
D	CYN808

site_id	BC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM A 142

Chain	Residue
A	TYR42
A	PHE43
A	PHE46
A	HIS58
A	LYS61
A	LEU83
A	LEU86
A	HIS87
A	LEU91
A	VAL93
A	ASN97
A	PHE98
A	LEU101
A	LEU136
A	CYN143
A	HOH1259
A	HOH1341
A	HOH1444
A	HOH1464
A	HOH1485
A	HOH1617
A	HOH1692

site_id	BC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM B 347

Chain	Residue
B	ASN102
B	LEU106
B	LEU141
B	CYN348
B	HOH1157
B	HOH1175
B	HOH1255
B	HOH1302
C	PRO4
C	ALA5
C	THR8
B	THR38
B	PHE41
B	PHE42
B	HIS63
B	LYS66
B	PHE71
B	LEU88
B	HIS92
B	LEU96
B	VAL98

site_id	BC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 542

Chain	Residue
C	TYR42
C	PHE43
C	HIS45
C	PHE46
C	HIS58
C	LYS61
C	LEU83
C	LEU86
C	HIS87
C	LEU91
C	VAL93
C	ASN97
C	PHE98
C	LEU101
C	LEU136
C	CYN543
C	HOH1284
C	HOH1633
C	HOH1698

site_id	BC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM D 747

Chain	Residue
D	THR38
D	PHE41
D	PHE42
D	HIS63
D	ALA70
D	HIS92
D	LEU96
D	VAL98
D	ASN102
D	PHE103
D	LEU106
D	LEU141
D	CYN748
D	HOH1107
D	HOH1131
D	HOH1587
D	HOH1609
D	HOH1695

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)