Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Z8U

Crystal structure of oxidized alpha hemoglobin bound to AHSP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005833	cellular_component	hemoglobin complex
A	0006457	biological_process	protein folding
A	0020027	biological_process	hemoglobin metabolic process
A	0030097	biological_process	hemopoiesis
A	0030218	biological_process	erythrocyte differentiation
A	0030492	molecular_function	hemoglobin binding
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
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	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	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
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005833	cellular_component	hemoglobin complex
C	0006457	biological_process	protein folding
C	0020027	biological_process	hemoglobin metabolic process
C	0030097	biological_process	hemopoiesis
C	0030218	biological_process	erythrocyte differentiation
C	0030492	molecular_function	hemoglobin binding
C	0050821	biological_process	protein stabilization
C	0051082	molecular_function	unfolded protein binding
D	0004601	molecular_function	peroxidase activity
D	0005344	molecular_function	oxygen carrier activity
D	0005506	molecular_function	iron ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0005833	cellular_component	hemoglobin complex
D	0006954	biological_process	inflammatory response
D	0015670	biological_process	carbon dioxide transport
D	0015671	biological_process	oxygen transport
D	0016020	cellular_component	membrane
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0030185	biological_process	nitric oxide transport
D	0031720	molecular_function	haptoglobin binding
D	0031838	cellular_component	haptoglobin-hemoglobin complex
D	0042542	biological_process	response to hydrogen peroxide
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0048821	biological_process	erythrocyte development
D	0070062	cellular_component	extracellular exosome
D	0071682	cellular_component	endocytic vesicle lumen
D	0072562	cellular_component	blood microparticle
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM B 201

Chain	Residue
B	PHE43
B	VAL93
B	ASN97
B	PHE98
B	LEU101
B	SER102
B	HOH203
B	HOH236
B	HOH243
D	MET76
D	PRO77
B	HIS45
D	ASN78
D	ALA79
B	PHE46
B	HIS58
B	LYS61
B	VAL62
B	ALA65
B	LEU83
B	HIS87

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D 201

Chain	Residue
B	MET76
B	PRO77
B	ASN78
B	ALA79
D	PHE43
D	HIS45
D	PHE46
D	HIS58
D	LYS61
D	VAL62
D	ALA65
D	LEU83
D	HIS87
D	LEU91
D	VAL93
D	ASN97
D	PHE98
D	LEU101
D	SER102
D	HOH204
D	HOH208
D	HOH227

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	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	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_FI5
Number of Residues	10
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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