6QYO
Structure of MBP-Mcl-1 in complex with compound 18a
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | Maltose/maltodextrin-binding periplasmic protein,Induced myeloid leukemia cell differentiation protein Mcl-1 | polymer | 518 | 57225.9 | 1 | UniProt (P0AEY0) UniProt (Q07820) Pfam (PF01547) Pfam (PF00452) UniProt (by SIFTS) (P0AEX9) In PDB | Escherichia coli | MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP,Bcl-2-like protein 3,Bcl2-L-3,Bcl-2-related protein EAT/mcl1,mcl1/EAT |
2 | B | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 342.3 | 1 | In PDB BIRD (PRD_900001) GlyTouCan (G07411ON) | alpha-maltose | ||
3 | A | (2~{R})-2-[5-[3-chloranyl-2-methyl-4-[2-(4-methylpiperazin-1-yl)ethoxy]phenyl]-6-ethyl-thieno[2,3-d]pyrimidin-4-yl]oxy-3-phenyl-propanoic acid | non-polymer | 595.2 | 1 | Chemie (JLH) | |||
4 | water | water | 18.0 | 250 | Chemie (HOH) |
Sequence modifications
A: -195 - 170 (UniProt: P0AEY0)
A: 173 - 321 (UniProt: Q07820)
PDB | External Database | Details |
---|---|---|
Met -196 | - | initiating methionine |
Ala -24 | Glu 198 | engineered mutation |
Ala -23 | Asn 199 | engineered mutation |
Ala 43 | Lys 265 | engineered mutation |
Gly 171 | - | linker |
Ser 172 | - | linker |
PDB | External Database | Details |
---|---|---|
Ala 194 | Lys 194 | engineered mutation |
Ala 197 | Lys 197 | engineered mutation |
Ala 201 | Arg 201 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 57225.9 | |
Branched | Number of molecules | 1 |
Total formula weight | 342.3 | |
Non-Polymers* | Number of molecules | 1 |
Total formula weight | 595.2 | |
All* | Total formula weight | 58163.3 |