2NRBA

C28s mutant of succinyl-coa:3-ketoacid coa transferase from pig heart
Total Genus 142
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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
142
sequence length
480
structure length
467
Chain Sequence
TKFYTDAVEAVKDIPNGATVLVGGFGLSGIPENLIGALLKTGVKELTAVSNNAGVDNFGLGLLLQSKQIKRMISSYVGENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSIAIASKPREVREFNGQHFILEEAIRGDFALVKAWKADQAGNVTFRKSARNFNLPMCKAAETTVVEVEEIVDIGSFAPEDIHIPKIYVHRLVKGEKYEKRIERLSVRKNVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGILGLGPYPLQNEVDADLINAGKETVTVLPGASYFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKLVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDRKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLIPMQQVT
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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 tags Transferase
source organism Sus scrofa
molecule keywords Succinyl-CoA:3-ketoacid-coenzyme A transferase 1
total genus 142
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 2nrbA01
3.40.1080.10 Alpha Beta 3-Layer(aba) Sandwich Glutaconate Coenzyme A-transferase Glutaconate Coenzyme A-transferase 2nrbA02
3RRLA 2AHVA 2NRBA 3OXOA 1OPEA 2AHWA 3QDQA 3RRLB 3DLXA 3CDKA 3D3UA 3K6MA 3GK7A 1XR4A 2AHUA 4KGBA 2HJ0A 1OOYA 1M3EA 2OASA 3CDKB 1POIA 5DBNA 1K6DA 1O9LA 3EH7A 1OOZA 1POIB 5DBNB 2NRCA
chains in the Genus database with same CATH superfamily
3RRLA 2AHVA 2NRBA 3OXOA 1OPEA 2AHWA 3QDQA 3RRLB 3DLXA 3CDKA 3D3UA 3K6MA 3GK7A 1XR4A 2AHUA 4KGBA 2HJ0A 1OOYA 1M3EA 2OASA 3CDKB 1POIA 5DBNA 1K6DA 1O9LA 3EH7A 1OOZA 1POIB 5DBNB 2NRCA
chains in the Genus database with same CATH topology
3RRLA 2AHVA 2NRBA 3OXOA 1OPEA 2AHWA 3QDQA 3RRLB 3DLXA 3CDKA 3D3UA 3K6MA 3GK7A 1XR4A 2AHUA 4KGBA 2HJ0A 1OOYA 1M3EA 2OASA 3CDKB 1POIA 5DBNA 1K6DA 1O9LA 3EH7A 1OOZA 1POIB 5DBNB 2NRCA
chains in the Genus database with same CATH homology


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