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4BHI

Three dimensional structure of human gamma-butyrobetaine hydroxylase in complex with 3-(1,1,1,2-Tetramethylhydrazin-1-ium-2-yl)propanoate

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
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 Residues12
DetailsBINDING SITE FOR RESIDUE OGA A 400
ChainResidue
AVAL183
ARUJ401
AZN402
AHOH2224
AALA193
ALEU199
AHIS202
AASP204
AHIS347
AARG349
AARG360
ALEU362

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RUJ A 401
ChainResidue
ATYR177
ATRP181
AASN191
ATYR194
AASP204
ATYR205
AASN292
ATHR295
ATYR366
AOGA400
AHOH2198
AHOH2211
AHOH2250

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AHIS202
AASP204
AHIS347
AOGA400

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
ACYS38
ACYS40
ACYS43
AHIS82

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 16D A 404
ChainResidue
ATYR75
ATYR75
ATYR83
ATYR83

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

218853

PDB entries from 2024-04-24

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