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1HMO

THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0015671biological_processoxygen transport
A0046872molecular_functionmetal ion binding
B0005344molecular_functionoxygen carrier activity
B0005506molecular_functioniron ion binding
B0015671biological_processoxygen transport
B0046872molecular_functionmetal ion binding
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0015671biological_processoxygen transport
C0046872molecular_functionmetal ion binding
D0005344molecular_functionoxygen carrier activity
D0005506molecular_functioniron ion binding
D0015671biological_processoxygen transport
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACE A 114
ChainResidue
AGLN60
ASER64

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO A 115
ChainResidue
AOXY116
AHIS25
AHIS54
AGLU58
AHIS73
AHIS77
AHIS101
AASP106

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OXY A 116
ChainResidue
AHIS25
AHIS54
APHE55
ALEU98
AHIS101
AASP106
AFEO115

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACE B 114
ChainResidue
BSER64
BHOH158
BHOH179

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO B 115
ChainResidue
BHIS25
BHIS54
BGLU58
BHIS73
BHIS77
BHIS101
BASP106
BOXY116

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OXY B 116
ChainResidue
BHIS25
BLEU28
BHIS54
BPHE55
BLEU98
BHIS101
BILE102
BASP106
BFEO115

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACE C 114
ChainResidue
CSER64
CHOH195

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO C 115
ChainResidue
CHIS25
CHIS54
CGLU58
CHIS73
CHIS77
CHIS101
CASP106
COXY116

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OXY C 116
ChainResidue
CHIS25
CHIS54
CPHE55
CLEU98
CHIS101
CILE102
CASP106
CFEO115

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACE D 114
ChainResidue
DGLN60
DSER64
DHOH282

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO D 115
ChainResidue
DHIS25
DHIS54
DGLU58
DHIS73
DHIS77
DHIS101
DASP106
DOXY116

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OXY D 116
ChainResidue
DHIS25
DHIS54
DPHE55
DLEU98
DHIS101
DILE102
DASP106
DFEO115

Functional Information from PROSITE/UniProt
site_idPS00550
Number of Residues24
DetailsHEMERYTHRINS Hemerythrin family signature. HFlnEQqlMqssq...Yagyae.HkkaH
ChainResidueDetails
AHIS54-HIS77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1870128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"678527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1870128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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