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2EF2

Crystal Structure of an Artificial Metalloprotein:Rh(Phebox-Ph)/apo-A71G 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 Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 2001
ChainResidue
AMET0
AHIS113
ASER117
AHOH2019

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 2002
ChainResidue
ALYS16
AHIS119

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 2003
ChainResidue
AHOH2013
AHOH2029
AILE112
AHIS113
AHOH2011

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE RHX A 1001
ChainResidue
ALEU29
APHE43
AHIS64
AVAL68
ALEU89
ASER92
AHIS93
ALEU104
AILE107
AGLU148
AHOH2092
AHOH2093

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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