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1HMD

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
A0098771biological_processinorganic ion homeostasis
B0005344molecular_functionoxygen carrier activity
B0005506molecular_functioniron ion binding
B0015671biological_processoxygen transport
B0046872molecular_functionmetal ion binding
B0098771biological_processinorganic ion homeostasis
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0015671biological_processoxygen transport
C0046872molecular_functionmetal ion binding
C0098771biological_processinorganic ion homeostasis
D0005344molecular_functionoxygen carrier activity
D0005506molecular_functioniron ion binding
D0015671biological_processoxygen transport
D0046872molecular_functionmetal ion binding
D0098771biological_processinorganic ion homeostasis
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
AHOH135
AHIS25
AHIS54
AGLU58
AHIS73
AHIS77
AHIS101
AASP106

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACE B 114
ChainResidue
BSER64
BHOH185

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FEO B 115
ChainResidue
BHIS25
BHIS54
BGLU58
BHIS73
BHIS77
BHIS101
BASP106

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACE C 114
ChainResidue
CSER64
CHOH211

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO C 115
ChainResidue
CHIS25
CHIS54
CGLU58
CHIS73
CHIS77
CHIS101
CASP106
CHOH147

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACE D 114
ChainResidue
DGLN60
DSER64
DHOH293

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FEO D 115
ChainResidue
DHIS25
DHIS54
DGLU58
DHIS73
DHIS77
DHIS101
DASP106

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: BINDING => ECO:0000269|PubMed:1870128, ECO:0000269|PubMed:678527, ECO:0007744|PDB:1HMD, ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ
ChainResidueDetails
AHIS25
BHIS101
CHIS25
CHIS54
CHIS73
CHIS77
CHIS101
DHIS25
DHIS54
DHIS73
DHIS77
AHIS54
DHIS101
AHIS73
AHIS77
AHIS101
BHIS25
BHIS54
BHIS73
BHIS77

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:1870128, ECO:0007744|PDB:1HMD, ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ
ChainResidueDetails
AGLU58
AASP106
BGLU58
BASP106
CGLU58
CASP106
DGLU58
DASP106

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PDB entries from 2024-07-31

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