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2V1I

Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 6.8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005737cellular_componentcytoplasm
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0016528cellular_componentsarcoplasm
A0019430biological_processremoval of superoxide radicals
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0098809molecular_functionnitrite reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A1154
ChainResidue
ATHR39
AHIS93
AHIS97
AILE99
ATYR103
ALEU104
AHIS113
AHIS116
AGLN128
AGOL1158
AHOH2102
ALYS42
AHOH2201
AHOH2202
AHOH2203
AHOH2204
AHOH2205
AHOH2212
APHE43
ALYS45
AHIS64
AVAL67
AVAL68
ALEU89
ASER92

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1156
ChainResidue
ATHR51
AGLU52
AHOH2088
AHOH2206

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1157
ChainResidue
AGLY1
AHOH2208
AHOH2209
AHOH2210

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A1158
ChainResidue
ALYS45
ALYS63
AHIS64
AHIS116
ASER117
AHEM1154
AGOL1159
AHOH2152
AHOH2204
AHOH2211

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A1159
ChainResidue
AARG31
ALYS45
AASP60
AHIS113
ASER117
AGOL1158
AHOH2053
AHOH2098
AHOH2212
AHOH2213
AHOH2214

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1160
ChainResidue
ASER3
AASP4
AGLY5
ALYS98
AHOH2215

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1161
ChainResidue
AARG31
AHIS36
ALYS96
AASP109
AALA110
AHOH2148
AHOH2217
AHOH2218
AHOH2219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02189, ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AHIS93

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76
ChainResidueDetails
ASER3

218853

PDB entries from 2024-04-24

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