1M7T

Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015035	molecular_function	protein-disulfide reductase activity

Functional Information from PROSITE/UniProt

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. VVdFSatWCGPCKmIkpfF

Chain	Residue	Details
A	VAL24-PHE42

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:9108029

Chain	Residue	Details
A	GLY33
A	LYS36

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Deprotonates C-terminal active site Cys => ECO:0000305

Chain	Residue	Details
A	PHE27

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Contributes to redox potential value => ECO:0000305

Chain	Residue	Details
A	PRO34
A	CYS35

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	GLN4
A	PRO40

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P10639

Chain	Residue	Details
A	THR9

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17260951

Chain	Residue	Details
A	GLN63

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	TYR69

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	PRO34
A	CYS35
A	CYS32
A	GLY33

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	CYS35
A	CYS32

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