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3U3E

Complex of Wild Type Myoglobin with Phenol in its Proximal Cavity

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 Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
ALYS42
AHIS97
AILE99
ATYR103
AIPH202
AHOH301
AHOH509
AHOH511
AHOH512
AHOH513
APHE43
AARG45
AHIS64
ATHR67
AVAL68
ALEU89
ASER92
AHIS93

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE IPH A 202
ChainResidue
ALEU89
AALA90
AHIS93
ALEU104
APHE138
AILE142
ATYR146
AHEM201

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AGLY124
AALA125
AASP126
AHOH514
AHOH517
AHOH518
AHOH519

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
ASER3
AGLU4
ATHR51
AGLU52
AALA53
AHOH318
AHOH532

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 205
ChainResidue
ASER3
AGLY5
AHOH318
AHOH321
AHOH322

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 206
ChainResidue
AARG45
ALYS63
AHIS64
ATHR67
AHOH396
AHOH511
AHOH523

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 207
ChainResidue
AALA19
AALA19
AALA19
AASP20
AHOH337
AHOH470

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN
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

218853

PDB entries from 2024-04-24

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