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3HF4

Crystal structure of rat methemoglobin in R2 state

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0001664molecular_functionG protein-coupled receptor binding
A0001701biological_processin utero embryonic development
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005833cellular_componenthemoglobin complex
A0006954biological_processinflammatory response
A0009617biological_processresponse to bacterium
A0015670biological_processcarbon dioxide transport
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0030185biological_processnitric oxide transport
A0031720molecular_functionhaptoglobin binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0032355biological_processresponse to estradiol
A0035634biological_processresponse to stilbenoid
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0045776biological_processnegative regulation of blood pressure
A0046872molecular_functionmetal ion binding
A0048821biological_processerythrocyte development
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005615cellular_componentextracellular space
B0005833cellular_componenthemoglobin complex
B0006749biological_processglutathione metabolic process
B0006954biological_processinflammatory response
B0015670biological_processcarbon dioxide transport
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030097biological_processhemopoiesis
B0030185biological_processnitric oxide transport
B0030492molecular_functionhemoglobin binding
B0031720molecular_functionhaptoglobin binding
B0031721molecular_functionhemoglobin alpha binding
B0031722molecular_functionhemoglobin beta binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0044877molecular_functionprotein-containing complex binding
B0046872molecular_functionmetal ion binding
B0048821biological_processerythrocyte development
B0070293biological_processrenal absorption
B0098869biological_processcellular oxidant detoxification
E0001540molecular_functionamyloid-beta binding
E0001664molecular_functionG protein-coupled receptor binding
E0001701biological_processin utero embryonic development
E0004601molecular_functionperoxidase activity
E0005344molecular_functionoxygen carrier activity
E0005506molecular_functioniron ion binding
E0005515molecular_functionprotein binding
E0005615cellular_componentextracellular space
E0005833cellular_componenthemoglobin complex
E0006954biological_processinflammatory response
E0009617biological_processresponse to bacterium
E0015670biological_processcarbon dioxide transport
E0015671biological_processoxygen transport
E0019825molecular_functionoxygen binding
E0020037molecular_functionheme binding
E0030185biological_processnitric oxide transport
E0031720molecular_functionhaptoglobin binding
E0031838cellular_componenthaptoglobin-hemoglobin complex
E0032355biological_processresponse to estradiol
E0035634biological_processresponse to stilbenoid
E0042542biological_processresponse to hydrogen peroxide
E0042744biological_processhydrogen peroxide catabolic process
E0045776biological_processnegative regulation of blood pressure
E0046872molecular_functionmetal ion binding
E0048821biological_processerythrocyte development
E0098869biological_processcellular oxidant detoxification
F0004601molecular_functionperoxidase activity
F0005344molecular_functionoxygen carrier activity
F0005615cellular_componentextracellular space
F0005833cellular_componenthemoglobin complex
F0006749biological_processglutathione metabolic process
F0006954biological_processinflammatory response
F0015670biological_processcarbon dioxide transport
F0015671biological_processoxygen transport
F0019825molecular_functionoxygen binding
F0020037molecular_functionheme binding
F0030097biological_processhemopoiesis
F0030185biological_processnitric oxide transport
F0030492molecular_functionhemoglobin binding
F0031720molecular_functionhaptoglobin binding
F0031721molecular_functionhemoglobin alpha binding
F0031722molecular_functionhemoglobin beta binding
F0031838cellular_componenthaptoglobin-hemoglobin complex
F0042542biological_processresponse to hydrogen peroxide
F0042744biological_processhydrogen peroxide catabolic process
F0044877molecular_functionprotein-containing complex binding
F0046872molecular_functionmetal ion binding
F0048821biological_processerythrocyte development
F0070293biological_processrenal absorption
F0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
AVAL93
AASN97
APHE98
ALEU101
AVAL132
AHOH144
APHE43
AHIS45
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87
ALEU91

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BTYR41
BPHE42
BHIS63
BLYS66
BVAL67
BLEU88
BHIS92
BVAL98
BASN102
BLEU106
BLEU141
BHOH149

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM E 142
ChainResidue
ETYR42
EPHE43
EHIS45
EHIS58
ELYS61
ELEU86
EHIS87
ELEU91
EVAL93
EASN97
EPHE98
ELEU101
EHOH143

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM F 147
ChainResidue
FTYR41
FPHE42
FHIS63
FLYS66
FVAL67
FLEU88
FHIS92
FLEU96
FVAL98
FASN102
FPHE103
FLEU106
FLEU141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsPeptide: {"description":"Hemopressin","featureId":"PRO_0000455938","evidences":[{"source":"PubMed","id":"12500972","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues424
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N-acetylvaline","evidences":[{"source":"UniProtKB","id":"P02086","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02088","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P11517","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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