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1FMF

REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0016853molecular_functionisomerase activity
A0016866molecular_functionintramolecular transferase activity
A0019553biological_processL-glutamate catabolic process via L-citramalate
A0019670biological_processanaerobic L-glutamate catabolic process
A0031419molecular_functioncobalamin binding
A0046872molecular_functionmetal ion binding
A0050097molecular_functionmethylaspartate mutase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues134
DetailsDomain: {"description":"B12-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00526","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00526","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
AASP14
AHIS16
AGLY67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
APHE27

246704

PDB entries from 2025-12-24

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