1L3X - JenaLib

Title :   SOLUTION STRUCTURE OF NOVEL DISINTEGRIN SALMOSIN

Authors :   J. Shin, W. Lee

Date :   01 Mar 02 (Deposition) - 23 Dec 03 (Release) - 21 Nov 12 (Revision)

Method :   SOLUTION NMR

Resolution :   NOT APPLICABLE

Chains :   NMR Structure  : A  (20x)
NMR Structure *: A  (1x)

Keywords :   Disintegrin, Snake Venome, Rgd, Protein Binding (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   J. Shin, S. Y. Hong, K. Chung, I. Kang, Y. Jang, D. S. Kim, W. Lee
Solution Structure Of A Novel Disintegrin, Salmosin, From Agkistrondon Halys Venom
Biochemistry V. 42 14408 2003
PubMed-ID: 14661951 | Reference-DOI: 10.1021/BI0300276

Compounds

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (0, 0)

Sites (0, 0)

SS Bonds (6, 6)

Cis Peptide Bonds (0, 0)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (1, 1)

Exons (0, 0)

Sequences/Alignments

NMR Structure

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Chain A from PDB  Type:PROTEIN  Length:73
 aligned with VM2HS_GLOBR | Q90WC0 from UniProtKB/Swiss-Prot  Length:317

    Alignment length:73
                                   254       264       274       284       294       304       314   
          VM2HS_GLOBR   245 EAGEECDCGSPGNPCCDAATCKLRQGAQCAEGLCCDQCRFMKEGTICRRARGDDLDDYCNGISAGCPRNPFHA 317
               SCOP domains d1l3xa_ A: Salmosin                                                       SCOP domains
               CATH domains 1l3xA00 A:1-73 Echistatin                                                 CATH domains
               Pfam domains ------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ......................................................................... Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------DISINTEGRIN_1       ------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------- Transcript
                 1l3x A   1 EAGEECDCGSPGNPCCDAATCKLRQGAQCAEGLCCDQCRFMKEGTICRRARGDDLDDYCNGISAGCPRNPFHA  73
                                    10        20        30        40        50        60        70

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Classification and Annotation

SCOP Domains (1, 1)

CATH Domains (1, 1)

Pfam Domains (0, 0)

Gene Ontology (7, 7)

NMR Structure(hide GO term definitions)

Chain A (VM2HS_GLOBR | Q90WC0)

molecular function
	GO:0016787	hydrolase activity	Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
	GO:0046872	metal ion binding	Interacting selectively and non-covalently with any metal ion.
	GO:0004222	metalloendopeptidase activity	Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
	GO:0008237	metallopeptidase activity	Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
	GO:0008233	peptidase activity	Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
biological process
	GO:0006508	proteolysis	The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
cellular component
	GO:0005576	extracellular region	The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

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