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1NWN

Crystals of CO-HbI in which the structure was converted to its unligated state, and then converted back to its original CO-ligated state.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005344molecular_functionoxygen carrier activity
A0005737cellular_componentcytoplasm
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0001666biological_processresponse to hypoxia
B0005344molecular_functionoxygen carrier activity
B0005737cellular_componentcytoplasm
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 147
ChainResidue
ATYR50
APHE111
ACMO148
BLYS96
BASN100
BHEM147
APHE51
AARG53
ALEU73
APHE97
AASN100
AHIS101
AARG104
AGLU110

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
ALYS96
AASN100
AHEM147
BTYR50
BPHE51
BARG53
BLEU73
BPHE97
BASN100
BHIS101
BARG104
BILE106
BGLU110
BPHE111
BCMO148
BHOH159
BHOH162

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO A 148
ChainResidue
AMET37
APHE51
AHIS69
ALEU73
AHEM147

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO B 148
ChainResidue
BMET37
BPHE51
BHIS69
BLEU73
BHEM147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: proximal binding residue
ChainResidueDetails
AHIS101
BHIS101

226707

PDB entries from 2024-10-30

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