4EQH

Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from human complexed with Trp-AMS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000118	cellular_component	histone deacetylase complex
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0005080	molecular_function	protein kinase C binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006508	biological_process	proteolysis
A	0006915	biological_process	apoptotic process
A	0007165	biological_process	signal transduction
A	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0009154	biological_process	purine ribonucleotide catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016926	biological_process	protein desumoylation
A	0016929	molecular_function	deSUMOylase activity
A	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
A	0050850	biological_process	positive regulation of calcium-mediated signaling
A	0070062	cellular_component	extracellular exosome
A	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator
B	0000118	cellular_component	histone deacetylase complex
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0005080	molecular_function	protein kinase C binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0006355	biological_process	regulation of DNA-templated transcription
B	0006508	biological_process	proteolysis
B	0006915	biological_process	apoptotic process
B	0007165	biological_process	signal transduction
B	0008233	molecular_function	peptidase activity
B	0008234	molecular_function	cysteine-type peptidase activity
B	0009154	biological_process	purine ribonucleotide catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016926	biological_process	protein desumoylation
B	0016929	molecular_function	deSUMOylase activity
B	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
B	0050850	biological_process	positive regulation of calcium-mediated signaling
B	0070062	cellular_component	extracellular exosome
B	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE WSA B 201

Chain	Residue
A	TRP123
B	GLY105
B	GLN106
B	SER107
B	VAL108
B	HIS112
B	HIS114
B	HOH327
B	HOH354
B	HOH355
B	HOH384
B	ILE18
B	HOH397
B	HOH399
B	PHE19
B	HIS42
B	ASP43
B	ILE44
B	SER45
B	LEU53
B	ASN99

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EPE B 202

Chain	Residue
B	THR17
B	THR17
B	ILE18
B	ILE18
B	SER107
B	HOH336
B	HOH336

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Functional Information from PROSITE/UniProt

site_id	PS00892
Number of Residues	19
Details	HIT_1 HIT domain signature. NegsdGgQsVyHVHLHVLG

Chain	Residue	Details
A	ASN99-GLY117

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	216
Details	Domain: {"description":"HIT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00464","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Motif: {"description":"Histidine triad motif"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"9323207","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22869114","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TW2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P70349","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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