Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2RAO

X ray crystal structure of rabbit hemoglobin (oxy form) at 2.0 angstrom 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	0005833	cellular_component	hemoglobin complex
A	0006417	biological_process	regulation of translation
A	0015671	biological_process	oxygen transport
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0031720	molecular_function	haptoglobin binding
A	0031838	cellular_component	haptoglobin-hemoglobin complex
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0043177	molecular_function	organic acid binding
A	0046872	molecular_function	metal ion binding
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	0005833	cellular_component	hemoglobin complex
B	0015671	biological_process	oxygen transport
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0031720	molecular_function	haptoglobin binding
B	0031721	molecular_function	hemoglobin alpha binding
B	0031838	cellular_component	haptoglobin-hemoglobin complex
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0043177	molecular_function	organic acid binding
B	0046872	molecular_function	metal ion binding
B	0072562	cellular_component	blood microparticle
B	0098869	biological_process	cellular oxidant detoxification
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	0005833	cellular_component	hemoglobin complex
C	0006417	biological_process	regulation of translation
C	0015671	biological_process	oxygen transport
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0031720	molecular_function	haptoglobin binding
C	0031838	cellular_component	haptoglobin-hemoglobin complex
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0043177	molecular_function	organic acid binding
C	0046872	molecular_function	metal ion binding
C	0072562	cellular_component	blood microparticle
C	0098869	biological_process	cellular oxidant detoxification
D	0004601	molecular_function	peroxidase activity
D	0005344	molecular_function	oxygen carrier activity
D	0005833	cellular_component	hemoglobin complex
D	0015671	biological_process	oxygen transport
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0031720	molecular_function	haptoglobin binding
D	0031721	molecular_function	hemoglobin alpha binding
D	0031838	cellular_component	haptoglobin-hemoglobin complex
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0043177	molecular_function	organic acid binding
D	0046872	molecular_function	metal ion binding
D	0072562	cellular_component	blood microparticle
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM A 142

Chain	Residue
A	TYR42
A	ASN97
A	PHE98
A	LEU136
A	OXY143
A	HOH164
A	HOH169
D	HIS2
A	PHE43
A	HIS45
A	HIS58
A	LYS61
A	LEU86
A	HIS87
A	LEU91
A	VAL93

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OXY A 143

Chain	Residue
A	HIS58
A	HEM142

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM B 147

Chain	Residue
B	THR38
B	PHE41
B	PHE42
B	HIS63
B	PHE71
B	HIS92
B	LEU96
B	ASN102
B	LEU106
B	LEU141
B	OXY148

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OXY B 148

Chain	Residue
B	HIS63
B	VAL67
B	HEM147

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OXY C 143

Chain	Residue
C	HIS58
C	HEM142

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 142

Chain	Residue
C	TYR42
C	PHE43
C	HIS45
C	PHE46
C	HIS58
C	LYS61
C	HIS87
C	LEU91
C	VAL93
C	ASN97
C	PHE98
C	LEU136
C	OXY143
C	HOH159
C	HOH193

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OXY D 148

Chain	Residue
D	HIS63
D	VAL67
D	LEU106
D	HEM147

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM D 147

Chain	Residue
A	THR8
A	LYS11
D	PHE41
D	PHE42
D	HIS63
D	LEU88
D	HIS92
D	LEU96
D	ASN102
D	OXY148
D	HOH172

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	568
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"description":"distal binding residue"}

Chain

Residue

Details

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

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
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)
		EDMap 2fo-fc (MTZ)