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4QUQ

Crystal structure of stachydrine demethylase in complex with azide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0044237biological_processcellular metabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 501
ChainResidue
ACYS86
AHIS88
AARG89
ASER91
ACYS106
AHIS109
AGLN110
ATRP111

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 502
ChainResidue
AHIS209
AASP360
AAZI505
AHIS204

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AARG15
ALEU16
AGLU22
AHOH612

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NCO A 504
ChainResidue
ALEU12
ALEU12
AASP13
AASP13
AARG15
AARG15
AGLU401
AHOH684
AHOH708

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE AZI A 505
ChainResidue
AASN199
AGLU201
ACYS202
AHIS209
AASP360
AFE502

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

218853

PDB entries from 2024-04-24

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