1FHI

SUBSTRATE ANALOG (IB2) COMPLEX WITH THE FRAGILE HISTIDINE TRIAD PROTEIN, FHIT

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001650	cellular_component	fibrillar center
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006163	biological_process	purine nucleotide metabolic process
A	0006915	biological_process	apoptotic process
A	0015964	biological_process	diadenosine triphosphate catabolic process
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
A	0042802	molecular_function	identical protein binding
A	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
A	0047352	molecular_function	adenylylsulfate-ammonia adenylyltransferase activity
A	0047627	molecular_function	adenylylsulfatase activity
A	0047710	molecular_function	bis(5'-adenosyl)-triphosphatase activity
A	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE IB2 A 301

Chain	Residue
A	GLN83
A	THR91
A	VAL92
A	HIS96
A	HIS98
A	LEU100
A	ARG102
A	PHE5
A	ILE10
A	ASN27
A	LEU37
A	THR79
A	SER81

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site_id	HIT
Number of Residues	3
Details	HIS 94, HIS 96, HIS 98 THE HISTIDINE TRIAD SITE CONTAINS THE MOTIF COMMON TO PROTEINS IN THE HIT SUPERFAMILY OF NUCLEOTIDE-BINDING PROTEINS. HIS 96 IS THE PRINCIPAL ACTIVE SITE RESIDUE AND SUBSTITUTION WITH ASN REDUCES KCAT (10E6)-FOLD WITH LITTLE EFFECT ON KM. HIS 98 IS PROPOSED TO H-BOND TO THE SCISSILE BRIDGING OXYGEN OF DINUCLEOTIDE SUBSTRATES.

Chain	Residue
A	HIS94
A	HIS96
A	HIS98

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLN83-PRO101

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Motif: {"description":"Histidine triad motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00464","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"15182206","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9323207","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9261067","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FIT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9323207","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FIT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15007172","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 5fit

Chain	Residue	Details
A	GLN83
A	HIS96
A	HIS94

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 101

Chain	Residue	Details
A	GLN83	electrostatic stabiliser, hydrogen bond donor
A	HIS94	electrostatic stabiliser, increase electrophilicity, increase nucleophilicity
A	HIS96	metal ligand, nucleofuge, nucleophile
A	HIS98	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

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