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3N6W

Crystal structure of human gamma-butyrobetaine hydroxylase

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS38
ACYS40
ACYS43
AHIS82

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AHOH561
AASN245
APRO246
AGLN247
AALA248
AGLU316

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ALEU45
AASP46
ASER47
ACYS267
AASP268
AARG375
AARG382

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
ALYS93
AARG94

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AARG101
APRO303
AHOH677

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
ALYS52
ALYS167
AARG168
AHOH653

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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