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8DYJ

Crystal structure of human methylmalonyl-CoA mutase in complex with ADP and cob(II)alamin

Functional Information from GO Data
ChainGOidnamespacecontents
B0003824molecular_functioncatalytic activity
B0003924molecular_functionGTPase activity
B0004494molecular_functionmethylmalonyl-CoA mutase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006790biological_processsulfur compound metabolic process
B0016853molecular_functionisomerase activity
B0016866molecular_functionintramolecular transferase activity
B0019678biological_processpropionate metabolic process, methylmalonyl pathway
B0031419molecular_functioncobalamin binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043547biological_processpositive regulation of GTPase activity
B0046872molecular_functionmetal ion binding
B0050667biological_processhomocysteine metabolic process
B0072341molecular_functionmodified amino acid binding
B1901290biological_processsuccinyl-CoA biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00544
Number of Residues26
DetailsMETMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS
ChainResidueDetails
BARG366-SER391

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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