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3G4Q

Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloroform bound to the XE4 cavity

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0042802molecular_functionidentical protein binding
B0005737cellular_componentcytoplasm
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 147
ChainResidue
ATYR50
AHOH157
AHOH167
AHOH182
AHOH184
AHOH205
AHOH223
BLYS96
BASN100
APHE51
AARG53
AHIS69
AHIS101
AARG104
AGLU110
APHE111
ACMO148

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO A 148
ChainResidue
AMET37
APHE51
AHIS69
ALEU73
AHEM147

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MCH A 151
ChainResidue
AVAL121
ATRP135

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
ALYS96
AASN100
AHOH182
BTYR50
BPHE51
BARG53
BLEU73
BPHE97
BHIS101
BARG104
BGLU110
BPHE111
BILE114
BCMO148
BMCH152
BHOH154
BHOH155
BHOH156
BHOH162
BHOH225

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO B 148
ChainResidue
BMET37
BPHE51
BHIS69
BLEU73
BHEM147

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MCH B 150
ChainResidue
BILE25
BLEU77
BILE118
BTRP135

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MCH B 152
ChainResidue
BLEU77
BPHE80
BPHE111
BVAL139
BVAL142
BHEM147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues274
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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