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4QUP

Crystal structure of stachydrine demethylase with N-methyl proline from low X-ray dose composite datasets

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 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
A3BY503
AHOH786
AHIS204
AHIS209
AASP360

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3BY A 503
ChainResidue
AASN199
AGLU201
ACYS202
AHIS204
ACYS205
AHIS209
ATHR356
AASP360
AFE502
AHOH786
AHOH860

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 504
ChainResidue
AARG14
AARG15
ALEU16
AGLU22
AHOH787
AHOH823
AHOH831

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
ATHR61
ALEU62
AARG63
AGLU68
ALYS95

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NCO A 506
ChainResidue
ALEU12
AASP13
AARG15
AHOH821
AHOH822

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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