2Z5H

Crystal structure of the head-to-tail junction of tropomyosin complexed with a fragment of TnT

Functional Information from GO Data

Chain	GOid	namespace	contents
T	0005861	cellular_component	troponin complex
T	0006937	biological_process	regulation of muscle contraction

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P58771","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P04692","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"278975","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	21
Details	Region: {"description":"Leucine-zipper","evidences":[{"source":"PROSITE-ProRule","id":"PRU00978","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1473154","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"624724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6993480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7622625","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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