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7RMP

Structure of ACLY D1026A - substrates-asym

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B, C, D
(A, B, C, D)
ATP-citrate synthasepolymer1101120940.14UniProt (P53396)
Pfam (PF24948)
Pfam (PF16114)
Pfam (PF02629)
Pfam (PF00549)
Pfam (PF00285)
Homo sapiens (human)ATP-citrate (pro-S-)-lyase,ACL,Citrate cleavage enzyme
2E, K, T
(A, B, D)
ADENOSINE-5'-DIPHOSPHATEnon-polymer427.23Chemie (ADP)
3F, L, U
(A, B, D)
(3S)-citryl-Coenzyme Anon-polymer941.63Chemie (Q5B)
4G, M, Q, V
(A, B, C, D)
CITRATE ANIONnon-polymer189.14Chemie (FLC)
5H, R
(A, C)
UNKNOWN LIGANDnon-polymer767.52Chemie (UNL)
6I, N, P, S
(A, B, C, D)
COENZYME Anon-polymer767.54Chemie (COA)
7J, O, W
(A, B, D)
PHOSPHATE IONnon-polymer95.03Chemie (PO4)
8AA, X, Y, Z
(D, A, B, C)
waterwater18.041Chemie (HOH)
Sequence modifications
A, B, C, D: 1 - 1101 (UniProt: P53396)
PDBExternal DatabaseDetails
Ala 1026Asp 1026engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains4
Total formula weight483760.5
Non-Polymers*Number of molecules19
Total formula weight9753.0
All*Total formula weight493513.5
*Water molecules are not included.

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PDB entries from 2026-01-21

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