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6X91

Crystal structure of MBP-fused human APOBEC1

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B, C, D, E...Maltodextrin-binding protein, C->U-editing enzyme APOBEC-1 chimerapolymer59367073.38UniProt (A0A4Z0THX4)
UniProt (P41238)
Pfam (PF01547)
Pfam (PF05240)
UniProt (by SIFTS) (P0AEX9)
In PDB
Escherichia coliApolipoprotein B mRNA-editing enzyme 1,HEPR,mRNA(cytosine(6666)) deaminase 1
2I, J, K, L, M...alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranosebranched342.314In PDB
BIRD (PRD_900001)
GlyTouCan (G07411ON)
alpha-maltose
3C, D, E, F, G...ZINC IONnon-polymer65.48Chemie (ZN)
4C, D, E, F, G...CACODYLATE IONnon-polymer137.08Chemie (CAC)
Sequence modifications
A, B, C, D, E, F, G, H: 2 - 367 (UniProt: A0A4Z0THX4)
PDBExternal DatabaseDetails
Met 1-initiating methionine
Val 313Ala 338engineered mutation
Asn 368-linker
Ser 369-linker
Ser 370-linker
Ser 371-linker
A, B, C, D, E, F, G, H: 1015 - 1236 (UniProt: P41238)
PDBExternal DatabaseDetails
Ala 1046Met 46engineered mutation
Ser 1048Arg 48engineered mutation
Ala 1063Glu 63engineered mutation
Thr 1080Met 80engineered mutation
Ala 1121Trp 121conflict
Asp 1146Ala 146engineered mutation
Ala 1173Leu 173engineered mutation
Ala 1199Trp 199engineered mutation
Ala 1205Phe 205engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains8
Total formula weight536586.5
BranchedNumber of molecules14
Total formula weight4792.2
Non-Polymers*Number of molecules16
Total formula weight1619.2
All*Total formula weight542997.8
*Water molecules are not included.

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PDB entries from 2024-07-17

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