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2G0S

Unphotolyzed CO-bound L29F Myoglobin, crystal 2

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 156
ChainResidue
ASER3
AGLU4
ALYS34
ATHR51
AGLU52
AHOH372

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 154
ChainResidue
ALEU89
ASER92
AHIS93
AHIS97
AILE99
ATYR103
ACMO155
AHOH233
AHOH271
AHOH272
AHOH317
AHOH323
ALYS42
APHE43
AARG45

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CMO A 155
ChainResidue
APHE29
AHIS64
AVAL68
AHEM154

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
AGLY65

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

217705

PDB entries from 2024-03-27

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