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3A2G

Crystal Structure of K102C-Myoglobin conjugated with Fluorescein

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 Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 154
ChainResidue
ALYS42
AHIS97
AILE99
ATYR103
ALEU104
AHOH178
AHOH192
AHOH202
AHOH236
AHOH254
AHOH255
APHE43
AARG45
AHIS64
ATHR67
AALA71
ALEU89
ASER92
AHIS93

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 155
ChainResidue
AARG45
AHIS64
ATHR67
AHOH254

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 156
ChainResidue
ALYS87
AGLY124
AALA125
AASP126
AGOL158
AHOH260
AHOH266

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 157
ChainResidue
ASER3
AGLU4
ATHR51
AGLU52
AALA53
AHOH185
AHOH232

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 158
ChainResidue
AGLY121
AASP122
APHE123
AGLY124
AASP126
AALA127
ASO4156
AHOH244
AHOH245

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LCY A 200
ChainResidue
APRO100
ACYS102
ATYR103
APHE106
AHOH219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959
ChainResidueDetails
AHIS93

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

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247
ChainResidueDetails
ATHR67

217705

数据于2024-03-27公开中

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