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3GQG

Crystal structure at acidic pH of the ferric form of the Root effect hemoglobin from Trematomus bernacchii.

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
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
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
C0098869biological_processcellular oxidant detoxification
D0005344molecular_functionoxygen carrier activity
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ATYR42
ALEU92
AVAL94
AASN98
APHE99
ALEU102
AHOH1512
APHE43
AHIS45
ATRP46
AHIS59
ALYS62
AVAL63
AGLN87
AHIS88

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM B 400
ChainResidue
BTHR38
BHIS41
BHIS63
BLYS66
BVAL67
BHIS92
BLEU96
BASN102
BPHE103
BLEU141

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM C 600
ChainResidue
CTYR42
CPHE43
CHIS45
CTRP46
CHIS59
CLYS62
CLEU84
CGLN87
CHIS88
CLEU92
CASN98
CPHE99
CLEU102
CLEU137
CHOH1485
CHOH1513

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM D 800
ChainResidue
DHIS41
DHIS63
DVAL67
DARG73
DLEU88
DLEU91
DHIS92
DLEU96
DASN102
DPHE103
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
BHIS63
DHIS63

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
BHIS92
DHIS92

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

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PDB entries from 2024-07-17

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