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2W6Y

Crystal structure of Sperm Whale Myoglobin mutant YQR in complex with Xenon

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 1154
ChainResidue
ATHR39
AHIS93
AHIS97
AILE99
ATYR103
AXE1158
AHOH2058
AHOH2205
AHOH2206
AHOH2207
AHOH2208
ALYS42
APHE43
AARG45
AGLN64
AARG67
AVAL68
ALEU89
ASER92

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1155
ChainResidue
AALA15
AALA15
ALYS16
ALYS16
ALYS16
AHOH2209
AHOH2209

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1156
ChainResidue
ALYS87
AGLY124
AALA125
AASP126
AHOH2210
AHOH2211
AHOH2212

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1157
ChainResidue
ASER3
AGLU4
ATHR51
AGLU52
AALA53
AHOH2213
AHOH2214
AHOH2215

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE XE A 1158
ChainResidue
ASER108
APHE138
AHEM1154

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE XE A 1160
ChainResidue
ALEU89
AHIS93

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE XE A 1161
ChainResidue
AHIS82
AALA134
APHE138
AHOH2119

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
AGLN64

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
AARG67

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PDB entries from 2024-04-24

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