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1FSL

FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009877biological_processnodulation
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0032025biological_processresponse to cobalt ion
A0046872molecular_functionmetal ion binding
A1901698biological_processresponse to nitrogen compound
A1904880biological_processresponse to hydrogen sulfide
B0005344molecular_functionoxygen carrier activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009877biological_processnodulation
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0032025biological_processresponse to cobalt ion
B0046872molecular_functionmetal ion binding
B1901698biological_processresponse to nitrogen compound
B1904880biological_processresponse to hydrogen sulfide
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM A 144
ChainResidue
APHE44
ALEU136
ANIO145
AHIS61
ALYS64
ALEU68
AVAL91
AHIS92
AGLN101
APHE102
ATYR133

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NIO A 145
ChainResidue
ATYR30
APHE44
APHE46
AHIS61
ALEU65
AHEM144

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM B 144
ChainResidue
BLEU43
BPHE44
BHIS61
BLYS64
BHIS92
BGLN101
BPHE102
BTYR133
BILE140
BNIO145
BHOH175

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NIO B 145
ChainResidue
BTYR30
BPHE44
BPHE46
BHIS61
BLEU65
BHEM144

Functional Information from PROSITE/UniProt
site_idPS00208
Number of Residues12
DetailsPLANT_GLOBIN Plant hemoglobins signature. NPkLtgHAeklF
ChainResidueDetails
AASN55-PHE66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02240
ChainResidueDetails
APHE46
AALA62
ALEU65
AALA96
BPHE46
BALA62
BLEU65
BALA96

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:29100196
ChainResidueDetails
AALA93
BALA93

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylvaline => ECO:0000269|PubMed:22308405
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Nitrated tyrosine => ECO:0000269|PubMed:25603991
ChainResidueDetails
ASER26
ATHR31
AASP134
BSER26
BTHR31
BASP134

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3C1F7
ChainResidueDetails
APHE46
BPHE46

227344

PDB entries from 2024-11-13

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