Brand  (β version)

PDB ID: 5YR6

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Ligands
Code Name Style Show Link
CO Cobalt (II) ion PoSSuM
NA Sodium ion PoSSuM
TN4 (1r,2s,3s,4r)-4-hydroxy-2-methoxy-4-methyl-3-[(2r,3r)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]cyclohexyl (chloroacetyl)carbamate PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 5YR6   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Human methionine aminopeptidase type 1b (F309L mutant) in complex with TNP470
Release Data : 2018-11-14
Compound :
mol_id molecule chains synonym
1 Methionine aminopeptidase 1 A MetAP 1,Peptidase M 1
ec: 3.4.11.18
fragment: UNP residues 81-384
mutation: F309L
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: METAP1
expression_system_strain: BL21(DE3)
Authors : Pillalamarri, V., Arya, T., Addlagatta, A.
Keywords : Metal binding protein, Methionine Aminopeptidase, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.7500 Å )
Citation :

Discovery of natural product ovalicin sensitive type 1 methionine aminopeptidases: molecular and structural basis.

Pillalamarri, V.,Arya, T.,Haque, N.  et al.
(2019)  Biochem. J.  476 : 991 - 1003

PubMed: 30837307
DOI: 10.1042/BCJ20180874

Reaction

Chain : A
UniProt : P53582 (MAP11_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. 3.4.11.18 HAMAP-Rule:MF_03174, PubMed:17114291
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Cofactor: Evidence: Note:
Fe(2+) ECO:0000255 | HAMAP-Rule:MF_03174
ECO:0000255 | HAMAP-Rule:MF_03174
ECO:0000255 | HAMAP-Rule:MF_03174
ECO:0000255 | HAMAP-Rule:MF_03174
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc