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3BIC

Crystal structure of human methylmalonyl-CoA mutase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003924molecular_functionGTPase activity
A0004494molecular_functionmethylmalonyl-CoA mutase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006790biological_processsulfur compound metabolic process
A0016853molecular_functionisomerase activity
A0016866molecular_functionintramolecular transferase activity
A0019678biological_processpropionate metabolic process, methylmalonyl pathway
A0031419molecular_functioncobalamin binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043547biological_processpositive regulation of GTPase activity
A0044281biological_processsmall molecule metabolic process
A0046872molecular_functionmetal ion binding
A0050667biological_processhomocysteine metabolic process
A0072341molecular_functionmodified amino acid binding
A1901290biological_processsuccinyl-CoA biosynthetic process
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
B0044281biological_processsmall molecule metabolic process
B0046872molecular_functionmetal ion binding
B0050667biological_processhomocysteine metabolic process
B0072341molecular_functionmodified amino acid binding
B1901290biological_processsuccinyl-CoA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 803
ChainResidue
ASER594
ALYS595

Functional Information from PROSITE/UniProt
site_idPS00544
Number of Residues26
DetailsMETMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS
ChainResidueDetails
AARG403-SER428

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues132
DetailsDomain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
AHIS627
AASP625
AHIS678

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
BHIS627
BASP625
BHIS678

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
ALYS621
AHIS265
AHIS627
ATYR110
AASP625

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
BLYS621
BHIS265
BHIS627
BTYR110
BASP625

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
APHE638

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
BPHE638

246704

PDB entries from 2025-12-24

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