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1NB0

Crystal Structure of Human Riboflavin Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006771biological_processriboflavin metabolic process
A0006915biological_processapoptotic process
A0008531molecular_functionriboflavin kinase activity
A0009231biological_processriboflavin biosynthetic process
A0009398biological_processFMN biosynthetic process
A0016301molecular_functionkinase activity
A0033864biological_processpositive regulation of NAD(P)H oxidase activity
A0046872molecular_functionmetal ion binding
A0072388biological_processflavin adenine dinucleotide biosynthetic process
A0072593biological_processreactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
ATHR34
AADP301
AHOH402
AHOH408

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP A 301
ChainResidue
APRO33
ATHR34
AASN36
ATHR87
AILE89
AHIS91
APHE93
AASP96
APHE97
ATYR98
AMG201
AHOH401
AHOH402
AHOH406
AHOH408
AHOH422
AHOH426
AHOH452
AVAL19
AGLY22
AGLY26
ASER27
ALYS28

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ALYS79

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12623014, ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0, ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M, ECO:0007744|PDB:1Q9S
ChainResidueDetails
ACYS15
AARG21
ALYS82
ASER84
AHIS91
AVAL104
AVAL107
ATYR109

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1Q9S
ChainResidueDetails
ASER27
AGLN29

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PDB entries from 2024-07-24

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