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2HMZ

THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

Replaces:  1HMZ
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 ACT A 114
ChainResidue
AGLN60
AALA64

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FEA A 115
ChainResidue
ATRP97
ALEU98
AHIS101
AILE102
AASP106
AHIS25
ALEU28
AHIS54
APHE55
AGLU58
AHIS73
AHIS77

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 114
ChainResidue
BGLN60
BALA64
BHOH178

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FEA B 115
ChainResidue
BHIS25
BLEU28
BHIS54
BPHE55
BGLU58
BHIS73
BHIS77
BTRP97
BLEU98
BHIS101
BILE102
BASP106

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT C 114
ChainResidue
CGLN60
CALA64
CHOH195

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FEA C 115
ChainResidue
CHIS25
CLEU28
CHIS54
CPHE55
CGLU58
CHIS73
CHIS77
CTRP97
CLEU98
CHIS101
CILE102
CASP106

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 114
ChainResidue
DGLN60
DALA64
DHOH282

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FEA D 115
ChainResidue
DHIS25
DLEU28
DHIS54
DPHE55
DGLU58
DHIS73
DHIS77
DTRP97
DLEU98
DHIS101
DILE102
DASP106

Functional Information from PROSITE/UniProt
site_idPS00550
Number of Residues24
DetailsHEMERYTHRINS Hemerythrin family signature. HFlnEQqlMqasq...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

246333

PDB entries from 2025-12-17

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