Structure of PDB 3som Chain P

Receptor sequence
>3somP (length=230) Species: 9606 (Homo sapiens) [Search protein sequence]
EPKVAELKQKIEDTLCPFGFEVYPFQVAWYNELLPPAFHLPLPGPTLAFL
VLSTPAMFDRALKPFLQSCHLRMLTDPVDQCVAYHLGRVRESLPELQIEI
IADYEVHPNRRPKILAQTAAHVAGAAYYYQRQDVEADPWGNQRISGVCIH
PRFGGWFAIRGVVLLPGIEVPDLPPRKPHDCVPTRADRIALLEGFNFHWR
DWTYRDAVTPQERYSEEQKAYFSTPPAQRL
3D structure
PDB3som Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function.
ChainP
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.16.1.6: cyanocobalamin reductase.
2.5.1.151: alkylcobalamin dealkylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 B12 P L34 L35 P36 D104 P113 A117 Q118 H122 Y129 Q131 R144 S146 C149 I160 F196 W200 L33 L34 P35 D103 P112 A116 Q117 H121 Y128 Q130 R143 S145 C148 I159 F195 W199
BS02 DHL P P152 C182 P151 C181
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0031419 cobalamin binding
GO:0032451 demethylase activity
GO:0033787 cyanocobalamin reductase (cyanide-eliminating) (NADP+) activity
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
GO:0071949 FAD binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0009235 cobalamin metabolic process
GO:0070988 demethylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3som, PDBe:3som, PDBj:3som
PDBsum3som
PubMed22642810
UniProtQ9Y4U1|MMAC_HUMAN Cyanocobalamin reductase / alkylcobalamin dealkylase (Gene Name=MMACHC)

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