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2MHR

STRUCTURE OF MYOHEMERYTHRIN IN THE AZIDOMET STATE AT 1.7(SLASH)1.3 ANGSTROMS RESOLUTION

Replaces:  1MHR
Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0015671biological_processoxygen transport
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AZI A 120
ChainResidue
AHIS25
AFEO119
AILE28
AHIS54
APHE55
ATRP102
ALEU103
AHIS106
AILE107
AASP111

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 124
ChainResidue
AGLU6
APRO7
ATYR8
APHE33
AILE36
AARG37
ALYS49
AHOH227
AHOH313

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 138
ChainResidue
ASER13
ATYR18
AGLU19
ALYS108
AHOH141
AHOH147
AHOH223
AHOH285
AHOH312

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 146
ChainResidue
ALEU87
ASER88
AVAL91
AASP92
AASN95
ALYS117
AHOH280
AHOH299

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO A 119
ChainResidue
AHIS25
AHIS54
AGLU58
AHIS73
AHIS77
AHIS106
AASP111
AAZI120

Functional Information from PROSITE/UniProt
site_idPS00550
Number of Residues24
DetailsHEMERYTHRINS Hemerythrin family signature. HFthEEamMdaak...Ysevvp.HkkmH
ChainResidueDetails
AHIS54-HIS77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3681996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2MHR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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