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1HBH

STRUCTURE OF DEOXYHAEMOGLOBIN OF THE ANTARCTIC FISH PAGOTHENIA BERNACCHII AND STRUCTURAL BASIS OF THE ROOT EFFECT

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
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
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005833cellular_componenthemoglobin complex
C0015671biological_processoxygen transport
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0031720molecular_functionhaptoglobin binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0042744biological_processhydrogen peroxide catabolic process
C0043177molecular_functionorganic acid binding
C0046872molecular_functionmetal ion binding
C0072562cellular_componentblood microparticle
D0004601molecular_functionperoxidase activity
D0005344molecular_functionoxygen carrier activity
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0031720molecular_functionhaptoglobin binding
D0031721molecular_functionhemoglobin alpha binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0042744biological_processhydrogen peroxide catabolic process
D0043177molecular_functionorganic acid binding
D0046872molecular_functionmetal ion binding
D0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 144
ChainResidue
AMET32
ALEU84
AHIS88
ALEU92
AASN98
ALEU137
ATYR42
APHE43
AHIS45
ATRP46
AHIS59
ALYS62
AVAL63
AILE67

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HEM B 148
ChainResidue
BHIS63
BVAL67
BLEU88
BHIS92
BLEU96
BVAL98
BASN102
BPHE103

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM C 144
ChainResidue
CTYR42
CHIS45
CHIS59
CLYS62
CVAL63
CLEU84
CGLN87
CHIS88
CLEU92
CVAL94
CASN98
CPHE99
CLEU137
CHOH157

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM D 148
ChainResidue
DTHR38
DHIS63
DLYS66
DVAL67
DLEU88
DHIS92
DLEU96
DASN102
DPHE103
DLEU106
DLEU141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0007744|PDB:1S5X, ECO:0007744|PDB:1S5Y, ECO:0007744|PDB:2PEG, ECO:0007744|PDB:4IRO
ChainResidueDetails
BGLY64
DGLY64

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:7623382, ECO:0007744|PDB:1HBH, ECO:0007744|PDB:1PBX, ECO:0007744|PDB:1S5X, ECO:0007744|PDB:1S5Y, ECO:0007744|PDB:2H8D, ECO:0007744|PDB:2H8F, ECO:0007744|PDB:2PEG, ECO:0007744|PDB:3GKV, ECO:0007744|PDB:3GQG, ECO:0007744|PDB:4G51, ECO:0007744|PDB:4IRO, ECO:0007744|PDB:4ODC
ChainResidueDetails
BSER93
DSER93

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7623382
ChainResidueDetails
ASER1
CSER1

218853

PDB entries from 2024-04-24

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