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1A6N

DEOXY-MYOGLOBIN, ATOMIC RESOLUTION

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 155
ChainResidue
AALA57
ASER58
AGLU59
AASP60
AHOH1007
AHOH1026
AHOH1038
AHOH1086

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 156
ChainResidue
ALYS62
AHOH1043
AHOH1045
AHOH1063
AGLN26

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 154
ChainResidue
ATHR39
ALYS42
APHE43
AARG45
AHIS64
ATHR67
AVAL68
AALA71
ALEU89
ASER92
AHIS93
AHIS97
AILE99
ATYR103
AHIS116
APHE138
AHOH1001
AHOH1024
AHOH1033
AHOH1059
AHOH1088
AHOH1092
AHOH1102
AHOH1118
AHOH1149

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
AGLY65

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
AALA94

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76
ChainResidueDetails
AGLU4

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247
ChainResidueDetails
AVAL68

218500

PDB entries from 2024-04-17

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