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2D2N

Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0005344molecular_functionoxygen carrier activity
B0005506molecular_functioniron ion binding
B0005576cellular_componentextracellular region
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0001666biological_processresponse to hypoxia
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005576cellular_componentextracellular region
C0005833cellular_componenthemoglobin complex
C0015671biological_processoxygen transport
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0005344molecular_functionoxygen carrier activity
D0005576cellular_componentextracellular region
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ALEU45
AARG97
ALEU99
AASN103
APHE104
AMET107
AILE138
AOXY201
DHIS91
DGLN95
APHE46
AVAL49
AHIS62
AVAL66
AALA69
ALEU90
AGLN93
AHIS94

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY A 201
ChainResidue
APHE32
AVAL66
AMET107
AHEM200

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
BPHE46
BARG48
BVAL49
BHIS62
BARG65
BVAL66
BLEU70
BGLN93
BHIS94
BARG97
BILE99
BGLY103
BTYR104
BPHE107
BOXY1201
BMMC1500
CHIS93
CGLN97

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OXY B 1201
ChainResidue
BTRP32
BPHE46
BHIS62
BVAL66
BHEM200

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM C 200
ChainResidue
BARG89
BGLN93
CLEU49
CPHE50
CGLY52
CHIS66
CARG69
CVAL70
CGLN97
CHIS98
CARG101
CVAL104
CHIS108
CPHE109
CMET112
CILE143
COXY2201

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY C 2201
ChainResidue
CHIS66
CVAL70
CHEM200

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM D 200
ChainResidue
AHIS89
AGLN93
DPHE39
DVAL45
DPHE50
DPRO51
DGLN64
DARG67
DVAL68
DGLN95
DHIS96
DALA106
DVAL107
DLEU110
DILE141
DOXY3201

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY D 3201
ChainResidue
DGLN64
DVAL68
DHEM200

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MMC A 500
ChainResidue
APHE32
APHE46
AVAL49
APHE59
AHIS62
ACYS63

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MMC B 1500
ChainResidue
BGLY69
BMET72
BCYS73
BLEU90
BILE140
BHEM200

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MMC C 2500
ChainResidue
CHIS66
CCYS67
CPHE36
CPHE50
CPHE63

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MMC D 3500
ChainResidue
DCYS3
DLEU79
DARG82
DCYS85
DTYR136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
DHIS96

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
CHIS98

223166

PDB entries from 2024-07-31

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