Information on 1ake_A_50 |
Loop code: 1ake_A_50 PDB: 1ake Chain: A Type: HH alpha-alpha |
Loop Start: 50 Loop Length: 5 Sec Struct Nt length: 6 Sec Struct Ct length: 13 Structure geometry
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Sequence: | KDIMDAGKLVTDELVIALVKERIA |
Sec Struct: | HHHHHHT----HHHHHHHHHHHHH |
PDB ligands within a cut-off distance of 6 Å in this loop |
Ligands | Residue | atSS | atLOOP |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | I - 52 | 1 | 0 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | M - 53 | 1 | 0 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | G - 56 | 0 | 1 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | K - 57 | 0 | 1 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | L - 58 | 0 | 1 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | V - 59 | 0 | 1 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | T - 60 | 0 | 1 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | D - 61 | 0 | 1 |
AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE | V - 64 | 1 | 0 |
Bibliographic Annotations |
Annotation | Residue | atSS | atLOOP |
REFERENCEC.W.MUELLER,G.E.SCHULZ. STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP=5=A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE J.MOL.BIOL. v.224;159,1992 | |||
AMP BINDING RESIDUE | D - 61 | 0 | 1 |
AMP BINDING RESIDUE | D - 61 | 0 | 1 |
Associated ArchDB-KI Subclass to 1ake_A_50 |