6SVA

Multicrystal structure of equine Haemoglobin at room temperature using a multilayer monochromator.

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	0005833	cellular_component	hemoglobin complex
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	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	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 201

Chain	Residue
A	TYR42
A	ASN97
A	PHE98
A	LEU101
A	LEU136
A	HOH305
A	HOH312
A	HOH332
A	PHE43
A	HIS45
A	HIS58
A	LYS61
A	LEU83
A	HIS87
A	LEU91
A	VAL93

---

site_id	AC2
Number of Residues	10
Details	binding site for residue HEM B 201

Chain	Residue
B	PHE41
B	PHE42
B	HIS63
B	SER70
B	PHE71
B	HIS92
B	ASN102
B	PHE103
B	LEU141
B	HOH305

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: distal binding residue => ECO:0000250|UniProtKB:P80044

Chain	Residue	Details
B	HIS63

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: proximal binding residue => ECO:0000269|PubMed:561852, ECO:0007744|PDB:1G0B, ECO:0007744|PDB:1IBE, ECO:0007744|PDB:1IWH, ECO:0007744|PDB:1NS6, ECO:0007744|PDB:1NS9, ECO:0007744|PDB:1Y8H, ECO:0007744|PDB:1Y8I, ECO:0007744|PDB:1Y8K, ECO:0007744|PDB:2D5X, ECO:0007744|PDB:2DHB, ECO:0007744|PDB:2MHB, ECO:0007744|PDB:2ZLT, ECO:0007744|PDB:2ZLU, ECO:0007744|PDB:2ZLV, ECO:0007744|PDB:2ZLW, ECO:0007744|PDB:2ZLX

Chain	Residue	Details
B	HIS92

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086

Chain	Residue	Details
B	VAL1
A	SER49

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	SER44
A	LYS11
A	LYS40

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	LYS59
B	LYS82
B	LYS144

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	CYS93

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905

Chain	Residue	Details
A	TYR24

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942

Chain	Residue	Details
A	SER102
A	SER124
A	SER131
A	SER138

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942

Chain	Residue	Details
A	THR108
A	THR134
A	THR137

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