2V1J

Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 8.7

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	27
Details	BINDING SITE FOR RESIDUE HEM A1154

Chain	Residue
A	ARG31
A	SER92
A	HIS93
A	HIS97
A	ILE99
A	TYR103
A	LEU104
A	HIS113
A	HIS116
A	GLN128
A	PHE138
A	THR39
A	GOL1158
A	HOH2188
A	HOH2189
A	HOH2190
A	HOH2191
A	HOH2192
A	HOH2193
A	HOH2194
A	LYS42
A	PHE43
A	LYS45
A	HIS64
A	VAL67
A	VAL68
A	LEU89

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A1156

Chain	Residue
A	LYS50
A	THR51
A	GLU52
A	HOH2195
A	HOH2196

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A1157

Chain	Residue
A	GLY1
A	HOH2004
A	HOH2199
A	HOH2200

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A1158

Chain	Residue
A	LYS45
A	HIS64
A	HIS116
A	SER117
A	HEM1154
A	HOH2089
A	HOH2192
A	HOH2201

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A1159

Chain	Residue
A	ARG31
A	HIS36
A	LYS96
A	PHE106
A	ASP109
A	ALA110
A	HOH2051
A	HOH2059
A	HOH2193
A	HOH2202

---

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

---