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3MS5

Crystal Structure of Human gamma-butyrobetaine,2-oxoglutarate dioxygenase 1 (BBOX1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008336molecular_functiongamma-butyrobetaine dioxygenase activity
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0042802molecular_functionidentical protein binding
A0045329biological_processcarnitine biosynthetic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 388
ChainResidue
AHIS202
AASP204
AHIS347
AOGA390
AHOH800

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 389
ChainResidue
ACYS38
ACYS40
ACYS43
AHIS82

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE OGA A 390
ChainResidue
AVAL183
AALA193
ALEU199
AHIS202
AASP204
AHIS347
AARG349
AARG360
ALEU362
ANI388
AREE391
AEDO393
AEDO395
AHOH800

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE REE A 391
ChainResidue
ATYR177
ATRP181
AASN191
ATYR194
AASP204
ATYR205
AASN292
ATYR366
AOGA390
AEDO393
AHOH418
AHOH485

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 392
ChainResidue
AHIS209
AGLU279
ATRP343
AHOH744

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 393
ChainResidue
AASN191
AALA193
ALEU199
AHIS202
AASN292
AOGA390
AREE391
AHOH457

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 394
ChainResidue
ALEU54
ALYS198
ALEU199
ASER200
AASN292
AASN293
AALA294
AHOH486
AHOH597
AHOH637

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 395
ChainResidue
ALEU217
ASER229
AHIS347
AGLY348
AOGA390

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 396
ChainResidue
ATYR173
ATYR173
ALEU174
ALEU174
AHOH556
AHOH556
AHOH590
AHOH590

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 397
ChainResidue
ATYR44
ALYS49
AALA50
ATHR260
AALA294
AARG296
ATHR298
AHOH421
AHOH528
AHOH799

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 398
ChainResidue
ALYS145
AASP341
ATRP369
AHOH517
AHOH733

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 399
ChainResidue
AGLN239
AGLY284
AGLN285
AVAL286

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 400
ChainResidue
ATRP33
AARG94
APHE96
AARG101
ATHR298
AILE299
APHE300
AHOH680

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ACYS38
ACYS40
ACYS43
AHIS82

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AHIS202
AASP204
AHIS347

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZU7
ChainResidueDetails
ASER351

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PDB entries from 2024-10-09

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