2NRCA

C28a mutant of succinyl-coa:3-ketoacid coa transferase from pig heart
Total Genus 143
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The genus trace: a function that shows values of genus (vertical axis) for subchains spanned between the first residue, and all other residues (shown on horizontal axis). The number of the latter residue and the genus of a given subchain are shown interactively.

Total Genus
143
sequence length
480
structure length
467
Chain Sequence
TKFYTDAVEAVKDIPNGATVLVGGFGLAGIPENLIGALLKTGVKELTAVSNNAGVDNFGLGLLLQSKQIKRMISSYVGENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSIAIASKPREVREFNGQHFILEEAIRGDFALVKAWKADQAGNVTFRKSARNFNLPMCKAAETTVVEVEEIVDIGSFAPEDIHIPKIYVHRLVKGEKYEKRIERLSVRKNVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGILGLGPYPLQNEVDADLINAGKETVTVLPGASYFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKLVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDRKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLIPMQQVT
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The genus matrix. At position (x,y) a genus value for a subchain spanned between x’th and y’th residue is shown. Values of the genus are represented by color, according to the scale given on the right.

Structure visualization

After clicking on a point (x,y) in the genus matrix above, a subchain from x to y is shown in color.

publication title Identification of the Cysteine Residue Exposed by the Conformational Change in Pig Heart Succinyl-CoA:3-Ketoacid Coenzyme A Transferase on Binding Coenzyme A.
pubmed doi rcsb
molecule keywords Succinyl-CoA:3-ketoacid-coenzyme A transferase 1
molecule tags Transferase
source organism Sus scrofa
total genus 143
structure length 467
sequence length 480
chains with identical sequence B, C, D
ec nomenclature ec 2.8.3.5: 3-oxoacid CoA-transferase.
pdb deposition date 2006-11-01

pfam database annotations

chain Pfam Accession Code Pfam Family Identifier Pfam Description
A PF01144 CoA_trans Coenzyme A transferase
Image from the rcsb pdb (www.rcsb.org)
cath code
ClassArchitectureTopologyHomologyDomain
3.40.1080.10 Alpha Beta 3-Layer(aba) Sandwich Glutaconate Coenzyme A-transferase Glutaconate Coenzyme A-transferase 2nrcA01
3.40.1080.10 Alpha Beta 3-Layer(aba) Sandwich Glutaconate Coenzyme A-transferase Glutaconate Coenzyme A-transferase 2nrcA02
1O9LA 2AHVA 1OOYA 1OOZA 1M3EA 2OASA 3QDQA 3RRLB 3K6MA 2HJ0A 5DBNB 3D3UA 3CDKA 1K6DA 1XR4A 3OXOA 3DLXA 1POIB 2NRBA 3RRLA 2AHUA 2NRCA 1OPEA 5DBNA 3GK7A 3EH7A 1POIA 2AHWA 4KGBA 3CDKB
chains in the Genus database with same CATH superfamily
1O9LA 2AHVA 1OOYA 1OOZA 1M3EA 2OASA 3QDQA 3RRLB 3K6MA 2HJ0A 5DBNB 3D3UA 3CDKA 1K6DA 1XR4A 3OXOA 3DLXA 1POIB 2NRBA 3RRLA 2AHUA 2NRCA 1OPEA 5DBNA 3GK7A 3EH7A 1POIA 2AHWA 4KGBA 3CDKB
chains in the Genus database with same CATH topology
1O9LA 2AHVA 1OOYA 1OOZA 1M3EA 2OASA 3QDQA 3RRLB 3K6MA 2HJ0A 5DBNB 3D3UA 3CDKA 1K6DA 1XR4A 3OXOA 3DLXA 1POIB 2NRBA 3RRLA 2AHUA 2NRCA 1OPEA 5DBNA 3GK7A 3EH7A 1POIA 2AHWA 4KGBA 3CDKB
chains in the Genus database with same CATH homology


 
#chains in the Genus database with same CATH superfamily
 1O9L A;  2AHV A;  1OOY A;  1OOZ A;  1M3E A;  2OAS A;  3QDQ A;  3RRL B;  3K6M A;  2HJ0 A;  5DBN B;  3D3U A;  3CDK A;  1K6D A;  1XR4 A;  3OXO A;  3DLX A;  1POI B;  2NRB A;  3RRL A;  2AHU A;  2NRC A;  1OPE A;  5DBN A;  3GK7 A;  3EH7 A;  1POI A;  2AHW A;  4KGB A;  3CDK B; 
#chains in the Genus database with same CATH topology
 1O9L A;  2AHV A;  1OOY A;  1OOZ A;  1M3E A;  2OAS A;  3QDQ A;  3RRL B;  3K6M A;  2HJ0 A;  5DBN B;  3D3U A;  3CDK A;  1K6D A;  1XR4 A;  3OXO A;  3DLX A;  1POI B;  2NRB A;  3RRL A;  2AHU A;  2NRC A;  1OPE A;  5DBN A;  3GK7 A;  3EH7 A;  1POI A;  2AHW A;  4KGB A;  3CDK B; 
#chains in the Genus database with same CATH homology
 1O9L A;  2AHV A;  1OOY A;  1OOZ A;  1M3E A;  2OAS A;  3QDQ A;  3RRL B;  3K6M A;  2HJ0 A;  5DBN B;  3D3U A;  3CDK A;  1K6D A;  1XR4 A;  3OXO A;  3DLX A;  1POI B;  2NRB A;  3RRL A;  2AHU A;  2NRC A;  1OPE A;  5DBN A;  3GK7 A;  3EH7 A;  1POI A;  2AHW A;  4KGB A;  3CDK B; 
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similar chains in the Genus database (?% sequence similarity)
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similar chains in the pdb database (?% sequence similarity)

 
#similar chains in the Genus database (?% sequence similarity)
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#similar chains, but unknotted
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