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6RP5

Crystal structure of monocarboxylated hemoglobin from the sub-Antarctic fish Eleginops maclovinus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031720molecular_functionhaptoglobin binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0042744biological_processhydrogen peroxide catabolic process
A0043177molecular_functionorganic acid binding
A0046872molecular_functionmetal ion binding
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031720molecular_functionhaptoglobin binding
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CMO A 201
ChainResidue
AVAL63
AHEM202

site_idAC2
Number of Residues17
Detailsbinding site for residue HEM A 202
ChainResidue
AHIS88
ALEU92
AVAL94
AASN98
ALEU102
ALEU137
ACMO201
AHOH310
AHOH319
BTYR49
AMET32
ATYR42
APHE43
AHIS45
ATRP46
ATHR62
ALEU84

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 203
ChainResidue
ATRP46
AHIS59
AHOH310
BASN50

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 204
ChainResidue
AVAL56
ALYS57
AALA58
AHOH367
BSER13
BHOH354

site_idAC5
Number of Residues5
Detailsbinding site for residue DTN A 205
ChainResidue
APRO51
AGLY52
AHOH401
BASN123
BPRO124

site_idAC6
Number of Residues3
Detailsbinding site for residue CMO B 201
ChainResidue
BHIS63
BVAL67
BHEM202

site_idAC7
Number of Residues12
Detailsbinding site for residue HEM B 202
ChainResidue
BHIS41
BLYS59
BHIS63
BLEU91
BHIS92
BLEU96
BPHE103
BLEU141
BCMO201
BHOH312
BHOH325
BHOH403

site_idAC8
Number of Residues12
Detailsbinding site for residue SO4 B 203
ChainResidue
BGLY43
BSER44
BPHE45
BGLY46
BASN57
BLYS59
BHOH314
BHOH317
BHOH318
BHOH362
BHOH388
BHOH402

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 B 204
ChainResidue
ALYS57
BSER17
BLYS117
BMET118
BHOH302
BHOH338

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue => ECO:0000269|PubMed:23086282
ChainResidueDetails
BHIS63

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:23086282
ChainResidueDetails
BHIS92

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000312|PDB:4ESA
ChainResidueDetails
ASER1

219869

PDB entries from 2024-05-15

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