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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
A0009791biological_processpost-embryonic development
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
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
B0009791biological_processpost-embryonic development
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 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 Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:20876572
ChainResidueDetails
AGLN50
BTYR96
BTHR106
BTHR216
BARG228
BLYS255
BHIS265
BARG304
ATYR96
ATHR106
ATHR216
AARG228
ALYS255
AHIS265
AARG304
BGLN50

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:20876572
ChainResidueDetails
AHIS627
BHIS627

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P16332
ChainResidueDetails
ALYS89
ALYS212
ALYS335
ALYS602
BLYS89
BLYS212
BLYS335
BLYS602

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P16332
ChainResidueDetails
ALYS343
ALYS595
BLYS343
BLYS595

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER481
BSER481

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

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PDB entries from 2024-07-24

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