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4OF9

Structure of K42N variant of sperm whale myoglobin

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 Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
APHE43
AILE99
ATYR103
AHOH301
AHOH302
AHOH324
AHOH327
AHOH337
AHOH402
AHOH458
AHOH527
AARG45
AHOH534
AHIS64
ATHR67
AVAL68
ALEU89
ASER92
AHIS93
AHIS97

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
ASER3
AGLU4
ATHR51
AGLU52
AALA53
AHOH330
AHOH477
AHOH481
AHOH482
AHOH559
AHOH593

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AARG45
ALYS63
AHIS64
ATHR67
AHOH337
AHOH435
AHOH533

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
AGLY124
AALA125
AASP126
AHOH311
AHOH368
AHOH428
AHOH446
AHOH523

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 205
ChainResidue
ASER3
AGLY5
AHOH330
AHOH412
AHOH481
AHOH484

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
AGLN26
ALYS56
ALYS62

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 207
ChainResidue
AALA94
ATHR95
AGLY150
ATYR151
AHOH373
AHOH552

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 208
ChainResidue
ALEU11
AALA15
AGLU18
ALYS77
AHOH437
AHOH439
AHOH452
AHOH476
AHOH488

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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