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4QUR

Crystal Structure of stachydrine demethylase in complex with cyanide, oxygen, and N-methyl proline in a new orientation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0044237biological_processcellular metabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 501
ChainResidue
ACYS86
AHIS88
AARG89
ACYS106
AHIS109
ATRP111

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 502
ChainResidue
AOXY506
ACYN507
AHIS204
AHIS209
AASP360

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 503
ChainResidue
AARG14
AARG15
ALEU16
AGLU22
APRO378
AHOH784
AHOH819
AHOH827

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NCO A 504
ChainResidue
ALEU12
ALEU12
AASP13
AASP13
AARG15
AARG15
AHOH817
AHOH817

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3BY A 505
ChainResidue
AASN199
AGLU201
ACYS202
APHE216
AALA223
ATRP305
AHIS307
ATRP353
AOXY506
ACYN507
AHOH646
AHOH854

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXY A 506
ChainResidue
AASN198
AHIS204
AHIS209
AASP360
AFE502
A3BY505

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CYN A 507
ChainResidue
AHIS204
AHIS209
AASP360
AFE502
A3BY505

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGslickarqGQvaklvCpYH
ChainResidueDetails
ACYS86-HIS109

226707

PDB entries from 2024-10-30

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