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2XIJ

Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin

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
Functional Information from PDB Data
site_idAC1
Number of Residues43
DetailsBINDING SITE FOR RESIDUE B12 A 800
ChainResidue
APHE138
AGLU392
AALA393
ALEU394
AGLY395
AGLN476
AGLY626
AHIS627
AASP628
AARG629
AGLY630
ALEU140
AILE634
AGLY670
ASER672
ALEU674
AALA675
AALA676
AGLY702
AGLY703
AVAL704
APHE722
AHIS143
AGLY723
APRO724
ATHR726
A5AD1746
AHOH2253
AHOH2447
AHOH2488
AHOH2508
AHOH3001
AHOH3002
AALA160
AHOH3003
AHOH3004
AHOH3005
AHOH3006
AVAL227
AARG228
ATHR230
AGLU268
ATRP356

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5AD A 1746
ChainResidue
AALA160
AGLN352
ALEU396
AHOH2173
AHOH2198
AHOH2252
AHOH2507
AHOH2508
AHOH2510
AB12800

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1747
ChainResidue
AARG613
AARG613
AARG614
AARG614
AARG616
AARG616
AHOH2511
AHOH2511

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1748
ChainResidue
ATYR146
AASN150
AARG152
AHOH2512

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1749
ChainResidue
ASER594
ALYS595
AGLU596
AHOH2513

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1750
ChainResidue
AGLU65
AASP272
AILE274
AHOH2035
AHOH2514
AHOH2515

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1751
ChainResidue
AASP58
AILE60
ATRP61
ALYS420
AHOH2030
AHOH2516

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1752
ChainResidue
AARG108
ASER306
AHIS350
ASER384

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1757
ChainResidue
ATHR249
AALA250
ASER258
AARG304
AHOH2190
AHOH2193

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1753
ChainResidue
AGLU117
AVAL510
AGLN514
ALYS517
AHOH2517

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1754
ChainResidue
ATHR216
AGLN218
ASER260
APHE308
ATYR110
ASER185
AMET186

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1755
ChainResidue
APRO695
AILE697
AHOH2485

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BTB A 1756
ChainResidue
AILE107
AARG108
AGLN109
ATYR110
AALA111
AGLN131
ASER135
AARG406
AHOH2079
AHOH2520
AHOH2521

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 Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20876572
ChainResidueDetails
ATYR96
ATHR106
ATHR216
AARG228
ALYS255
AHIS265
AARG304
AGLN50

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:20876572
ChainResidueDetails
AHIS627

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P16332
ChainResidueDetails
ALYS89
ALYS212
ALYS335
ALYS602

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P16332
ChainResidueDetails
ALYS343
ALYS595

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER481

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PDB entries from 2024-04-17

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