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1N08

Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005829cellular_componentcytosol
A0006771biological_processriboflavin metabolic process
A0008270molecular_functionzinc ion binding
A0008531molecular_functionriboflavin kinase activity
A0009231biological_processriboflavin biosynthetic process
A0009398biological_processFMN biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046872molecular_functionmetal ion binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005829cellular_componentcytosol
B0006771biological_processriboflavin metabolic process
B0008270molecular_functionzinc ion binding
B0008531molecular_functionriboflavin kinase activity
B0009231biological_processriboflavin biosynthetic process
B0009398biological_processFMN biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ASER38
ATHR45
AADP301
AHOH569
AHOH640

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 601
ChainResidue
BSER38
BTHR45
BASN47
BADP401

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP A 301
ChainResidue
AVAL30
AHIS32
AGLY33
AGLY35
AGLY37
ASER38
ALYS39
APRO44
ATHR45
AALA46
AVAL97
ALEU99
AARG102
AASP106
APHE107
ATYR108
AZN501
AHOH504
AHOH529
AHOH553
AHOH622
BTYR88

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP B 401
ChainResidue
ATYR88
BGLY35
BARG36
BGLY37
BSER38
BLYS39
BPRO44
BTHR45
BALA46
BVAL97
BHIS98
BLEU99
BARG102
BASP106
BPHE107
BTYR108
BZN601
BHOH609
BHOH615
BHOH616
BHOH643
BHOH645
BHOH652
BHOH657
BHOH666
BHOH688

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
AGLU96
BGLU96

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATHR45
BTHR45

223790

PDB entries from 2024-08-14

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