2QKV - JenaLib

Asymmetric Unit

Reformat:	Number of residues per line = ('0' or empty: single-line sequence representation)
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	UniProt sequence: complete aligned part

Show mapping:	SCOP domains	CATH domains	Pfam domains	Secondary structure (by author)
	SAPs(SNPs)	PROSITE motifs	Exons
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Chain A from PDB  Type:PROTEIN  Length:92
 aligned with INAD_DROME | Q24008 from UniProtKB/Swiss-Prot  Length:674

    Alignment length:123
                                   552       562       572       582       592       602       612       622       632       642       652       662   
           INAD_DROME   543 GTPIHVGSMTTLKVHQLFHTTYEKAVTLTVFRADPPELEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVCYALFKGANGKVSMEVTRPKP 665
               SCOP domains --------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ......-------------------------------...eeeeee........eeeee....eeeeee....hhhhhhhh....eeeee..ee....hhhhhhhhhhh...eeeeeee.... Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE PDZ  PDB: -------------------------------PDZ  PDB: A:584-664 UniProt: 584-664                                             - PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------- Transcript
                 2qkv A 574 GIPRNS-------------------------------LEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVSYALFKGANGKVSMEVTRPKP 665
                                 |   -         -         -       582       592       602       612       622       632       642       652       662   
                               579                             580

Chain B from PDB  Type:PROTEIN  Length:92
 aligned with INAD_DROME | Q24008 from UniProtKB/Swiss-Prot  Length:674

    Alignment length:123
                                   552       562       572       582       592       602       612       622       632       642       652       662   
           INAD_DROME   543 GTPIHVGSMTTLKVHQLFHTTYEKAVTLTVFRADPPELEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVCYALFKGANGKVSMEVTRPKP 665
               SCOP domains --------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------- CATH domains
           Pfam domains (1) -----------------------------------------PDZ-2qkvB01 B:584-661                                                         ---- Pfam domains (1)
           Pfam domains (2) -----------------------------------------PDZ-2qkvB02 B:584-661                                                         ---- Pfam domains (2)
         Sec.struct. author ......-------------------------------..eeeeeeee.......eeeeee..eeeeeee....hhhhhhhh....eeeee..ee....hhhhhhhhhhh..eeeeeeee.... Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE PDZ  PDB: -------------------------------PDZ  PDB: B:584-664 UniProt: 584-664                                             - PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------- Transcript
                 2qkv B 574 GIPRNS-------------------------------LEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVSYALFKGANGKVSMEVTRPKP 665
                                 |   -         -         -       582       592       602       612       622       632       642       652       662   
                               579                             580

Legend:		→ Mismatch	(orange background)
	-	→ Gap	(green background, '-', border residues have a numbering label)
		→ Modified Residue	(blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
	x	→ Chemical Group	(purple background, 'x', labelled with number + name, e.g. ACE or NH2)
	extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '\|'

Classification and Annotation

SCOP Domains (0, 0)

CATH Domains (0, 0)

Pfam Domains (1, 2)

Gene Ontology (19, 19)

Asymmetric Unit(hide GO term definitions)

Chain A,B (INAD_DROME | Q24008)

molecular function
	GO:0005516	calmodulin binding	Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
	GO:0031473	myosin III binding	Interacting selectively and non-covalently with a class III myosin; myosin III is monomeric and has an N terminal kinase domain.
	GO:0017022	myosin binding	Interacting selectively and non-covalently with any part of a myosin complex; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments.
	GO:0009881	photoreceptor activity	The function of absorbing and responding to incidental electromagnetic radiation, particularly visible light. The response may involve a change in conformation.
	GO:0005515	protein binding	Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
	GO:0030159	receptor signaling complex scaffold activity	Functions to provide a physical support for the assembly of a multiprotein receptor signaling complex.
	GO:0005198	structural molecule activity	The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.
biological process
	GO:0071482	cellular response to light stimulus	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a light stimulus, electromagnetic radiation of wavelengths classified as infrared, visible or ultraviolet light.
	GO:0016059	deactivation of rhodopsin mediated signaling	The process of restoring the photoreceptor cell to its unexcited state after termination of the stimulus (photon).
	GO:0050962	detection of light stimulus involved in sensory perception	The series of events in which a light stimulus is received by a cell and converted into a molecular signal as part of the sensory perception of light.
	GO:0007602	phototransduction	The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
	GO:0008104	protein localization	Any process in which a protein is transported to, or maintained in, a specific location.
	GO:0050896	response to stimulus	Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. The process begins with detection of the stimulus and ends with a change in state or activity or the cell or organism.
	GO:0007605	sensory perception of sound	The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
	GO:0007601	visual perception	The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
cellular component
	GO:0016027	inaD signaling complex	A complex of proteins that are involved in phototransduction and attached to the transient receptor potential (TRP) channel. The protein connections are mediated through inaD.
	GO:0016020	membrane	A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
	GO:0005886	plasma membrane	The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
	GO:0016028	rhabdomere	The specialized microvilli-containing organelle on the apical surfaces of a photoreceptor cell containing the visual pigment rhodopsin and most of the proteins involved in phototransduction.

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	Ligands, Modified Residues, Ions
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	Sites
(no "Sites" information available for 2qkv)

	Cis Peptide Bonds
(no "Cis Peptide Bonds" information available for 2qkv)

Biological Unit
	Complete Structure
		Biological Unit 1	[ Jena3D ]

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Databases and Analysis Tools

Databases

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	2qkv
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	INAD_DROME \| Q24008
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Description

Compounds

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (0, 0)

Sites (0, 0)

SS Bonds (0, 0)

Cis Peptide Bonds (0, 0)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (1, 2)

Exons (0, 0)

Sequences/Alignments