2VLZ

Crystal structure of peroxymyoglobin generated by cryoradiolytic reduction of myoglobin compound III

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005344	molecular_function	oxygen carrier activity
A	0005737	cellular_component	cytoplasm
A	0015671	biological_process	oxygen transport
A	0016491	molecular_function	oxidoreductase activity
A	0016528	cellular_component	sarcoplasm
A	0019430	biological_process	removal of superoxide radicals
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0098809	molecular_function	nitrite reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM A 1154

Chain	Residue
A	THR39
A	ILE99
A	TYR103
A	LEU104
A	HIS113
A	HIS116
A	GLN128
A	PER1155
A	HOH2152
A	HOH2153
A	HOH2154
A	LYS42
A	HOH2155
A	HOH2156
A	HOH2166
A	PHE43
A	LYS45
A	VAL68
A	LEU89
A	SER92
A	HIS93
A	HIS97

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PER A 1155

Chain	Residue
A	PHE43
A	HIS64
A	VAL68
A	HEM1154

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1156

Chain	Residue
A	THR51
A	GLU52
A	HOH2158
A	HOH2159

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1157

Chain	Residue
A	GLY1
A	HOH2160
A	HOH2161
A	HOH2162

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1158

Chain	Residue
A	ARG31
A	LYS45
A	HIS113
A	SER117
A	HOH2070
A	HOH2163
A	HOH2165
A	HOH2166

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEO A 1159

Chain	Residue
A	GLY1
A	LEU2
A	TRP7
A	LEU137
A	HOH2167

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEO A 1160

Chain	Residue
A	LEU40
A	LEU49
A	LYS50
A	HOH2063
A	HOH2168

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEO A 1161

Chain	Residue
A	ARG31
A	LYS96
A	ALA110
A	HOH2169

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEO A 1162

Chain	Residue
A	VAL67
A	HIS116
A	HIS119
A	GLY121
A	ASP122
A	PHE123
A	HOH2170

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEO A 1163

Chain	Residue
A	LYS16
A	ALA19
A	HIS24
A	HIS119
A	HOH2171
A	HOH2173

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P02189, ECO:0000255|PROSITE-ProRule:PRU00238

Chain	Residue	Details
A	HIS64

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: proximal binding residue => ECO:0000269|PubMed:10706294, ECO:0000269|PubMed:2359126, ECO:0000269|PubMed:7654702, ECO:0007744|PDB:1AZI, ECO:0007744|PDB:1BJE, ECO:0007744|PDB:1DWR, ECO:0007744|PDB:1DWS, ECO:0007744|PDB:1DWT, ECO:0007744|PDB:1GJN, ECO:0007744|PDB:1HSY, ECO:0007744|PDB:1NPF, ECO:0007744|PDB:1NPG, ECO:0007744|PDB:1NZ2, ECO:0007744|PDB:1NZ3, ECO:0007744|PDB:1NZ4, ECO:0007744|PDB:1NZ5, ECO:0007744|PDB:1RSE, ECO:0007744|PDB:1WLA, ECO:0007744|PDB:1XCH, ECO:0007744|PDB:1YMA, ECO:0007744|PDB:1YMB, ECO:0007744|PDB:2FRF, ECO:0007744|PDB:2FRI, ECO:0007744|PDB:2FRJ, ECO:0007744|PDB:2FRK, ECO:0007744|PDB:2NSR, ECO:0007744|PDB:2NSS, ECO:0007744|PDB:2V1E, ECO:0007744|PDB:2V1F, ECO:0007744|PDB:2V1G, ECO:0007744|PDB:2V1H, ECO:0007744|PDB:2V1I, ECO:0007744|PDB:2V1J, ECO:0007744|PDB:2V1K, ECO:0007744|PDB:2VLX, ECO:0007744|PDB:2VLY, ECO:0007744|PDB:2VLZ, ECO:0007744|PDB:2VM0, ECO:0007744|PDB:3HC9, ECO:0007744|PDB:3HEN, ECO:0007744|PDB:3HEO, ECO:0007744|PDB:3HEP, ECO:0007744|PDB:3LR7, ECO:0007744|PDB:3LR9, ECO:0007744|PDB:3RJ6, ECO:0007744|PDB:3VM9, ECO:0007744|PDB:3WYO, ECO:0007744|PDB:4DC7, ECO:0007744|PDB:4DC8, ECO:0007744|PDB:4NS2

Chain	Residue	Details
A	HIS93

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76

Chain	Residue	Details
A	SER3

---