1FSX

THE X-RAY STRUCTURE DETERMINATION OF BOVINE CARBONMONOXY HB AT 2.1 A RESOLUTION AND ITS RELATIONSHIP TO THE QUATERNARY STRUCTURE OF OTHER HB CRYSTAL FORMS

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0015671	biological_process	oxygen transport
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0031838	cellular_component	haptoglobin-hemoglobin complex
A	0046872	molecular_function	metal ion binding
A	0048821	biological_process	erythrocyte development
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	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
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	0015671	biological_process	oxygen transport
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0031838	cellular_component	haptoglobin-hemoglobin complex
C	0046872	molecular_function	metal ion binding
C	0048821	biological_process	erythrocyte development
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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CMO A 142

Chain	Residue
A	HIS58
A	VAL62
A	HEM143

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM A 143

Chain	Residue
A	LEU91
A	VAL93
A	ASN97
A	PHE98
A	LEU101
A	VAL132
A	LEU136
A	CMO142
A	HOH830
A	HOH854
A	TYR42
A	HIS45
A	HIS58
A	LYS61
A	LEU66
A	HIS87

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CMO B 347

Chain	Residue
B	HIS263
B	VAL267
B	HEM348

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM B 348

Chain	Residue
B	THR238
B	PHE241
B	PHE242
B	HIS263
B	LYS266
B	SER270
B	LEU291
B	HIS292
B	LEU296
B	VAL298
B	ASN302
B	PHE303
B	CMO347
B	HOH930
D	LYS608

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CMO C 542

Chain	Residue
C	HIS458
C	VAL462
C	HEM543

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 543

Chain	Residue
C	TYR442
C	PHE443
C	HIS445
C	HIS458
C	LYS461
C	GLU482
C	HIS487
C	LEU491
C	VAL493
C	ASN497
C	PHE498
C	LEU501
C	LEU536
C	CMO542
C	HOH877

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CMO D 747

Chain	Residue
D	HIS663
D	VAL667
D	HEM748

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM D 748

Chain	Residue
C	ALA404
D	PHE641
D	PHE642
D	HIS663
D	LYS666
D	VAL667
D	SER670
D	LEU688
D	HIS692
D	LEU696
D	VAL698
D	ASN702
D	PHE703
D	LEU706
D	LEU741
D	CMO747

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Peptide: {"description":"Hemopressin","featureId":"PRO_0000455842","evidences":[{"source":"UniProtKB","id":"P01946","evidenceCode":"ECO:0000250"}]}

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	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
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_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	12
Details	Peptide: {"description":"Spinorphin","featureId":"PRO_0000424225"}

Chain

Residue

Details

---

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

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Binding site: {"description":"proximal binding residue"}

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	4
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

---