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3TLD

Crystal Structure of Y29F mutant of Vitreoscilla hemoglobin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046210biological_processnitric oxide catabolic process
A0046872molecular_functionmetal ion binding
A0071500biological_processcellular response to nitrosative stress
A0071949molecular_functionFAD binding
B0005344molecular_functionoxygen carrier activity
B0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046210biological_processnitric oxide catabolic process
B0046872molecular_functionmetal ion binding
B0071500biological_processcellular response to nitrosative stress
B0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
ALEU42
AVAL90
AHIS94
ATYR95
AVAL98
APHE133
AHOH302
AHOH321
AHOH330
AHOH392
AHOH414
APHE43
APRO54
ALEU57
ATHR60
AVAL61
AILE81
ALYS84
AHIS85

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
AASP112
AHOH405
AHOH415

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 201
ChainResidue
BLEU42
BPHE43
BPRO54
BLEU57
BTHR60
BVAL61
BILE81
BLYS84
BHIS85
BVAL90
BHIS94
BTYR95
BVAL98
BTYR126
BHOH327
BHOH334
BHOH340
BHOH381

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 202
ChainResidue
BHOH400

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 203
ChainResidue
APRO76
BASP139
BGLN143
BHOH407

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AGLN53
BGLN53

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS85
BHIS85

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PDB entries from 2024-06-12

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