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2EB9

Crystal Structure of Cu(II)(Sal-Leu)/apo-Myoglobin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
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
ALYS16
AARG118
AHIS119
AHOH3075

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 2002
ChainResidue
AHOH3025
AHOH3093
AMET0
AHIS113
ASER117
AHOH3003
AHOH3014

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 2003
ChainResidue
AARG45
AGLU83
AHIS116
ALYS145
AGLU148
AHOH3012
AHOH3092

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 2004
ChainResidue
AHIS12
ALYS16
ALYS47
AASP122
AHOH3020

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 2005
ChainResidue
ALYS42
ALYS62
ALYS102
AHOH3022
AHOH3026
AHOH3063

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CUS A 1001
ChainResidue
ALEU32
APHE43
AHIS64
AVAL68
ALEU89
AHIS93

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 3001
ChainResidue
AASP44
AARG45
AHIS48
AASP60
AGLY121
AASP122
APHE123
AGLY124
AALA125
AASP126
AALA127
AHOH3124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7463482","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MBO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"845959","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MBN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MBN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QZ76","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04247","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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