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Information on SUBCLASS 4.21.1
Subclass Accession number: 6790
Subclass: 4.21.1 PSSM
Type: AR beta-beta link
DB: ArchDB-EC

Image coordinates: Rasmol PDB Jmol PDB
Consensus coordinates: Rasmol PDB Jmol PDB
Number of loops: 4

Average sequence ID (%) : 12.5 +/- 17.8
Average RMSD (Å) : 1.275 +/- 0.275

Consensus geometry
d (Å): 11 delta (°): 90-135 theta (°): 135-180 rho (°): 0-45
Consensus Sequence: XXXphXXp
(φψ)-conformation: bbaappbb
Pattern: xx[IMV]x[APS]x[DHS][VY]xx[AEST][IW]
Conservation:-1.052-0.4121.513-0.9100.291-1.2650.4711.055-1.3371.098-0.1980.745
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1aoe_A_731aoe   A7485NIILSRSYENEIEEEE-TT---EExbbbbaaxxxbx
1ar1_B_1701ar1   B172183VQVTATDVIHAWEEEEESSS-EEEbbxbbaabxbbx
1svp_A_1351svp   A135146KVMKPLHVKGTIEEEEETT--SEEbxbbxaaxxbbx
2occ_B_1502occ   B152163MLVSSEDVLHSWEEEEESSS-EEEbbbbbaaxxbbx
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1aoe_A_731aoe   A     NDPNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE L - 77
1aoe_A_731aoe   A     NDPNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE S - 78
1aoe_A_731aoe   A     NDPNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE R - 79
1aoe_A_731aoe   A     NDPNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE S - 80
1ar1_B_1701ar1   B     CUCOPPER (II) ION I - 180
1ar1_B_1701ar1   B     CUCOPPER (II) ION H - 181
1ar1_B_1701ar1   B     CUCOPPER (II) ION A - 182
1ar1_B_1701ar1   B     MGMAGNESIUM ION A - 182
2occ_B_1502occ   B     CUCOPPER (II) ION V - 159
2occ_B_1502occ   B     CUCOPPER (II) ION L - 160
2occ_B_1502occ   B     CUCOPPER (II) ION H - 161
2occ_B_1502occ   B     CUCOPPER (II) ION S - 162
2occ_B_1502occ   B     MGMAGNESIUM ION S - 162
PDB Site Annotated loops in this subclass
LoopPDBChainSiteResidue
1ar1_B_1701ar1   B CUACU A BINDING SITE.H - 181
1svp_A_1351svp   A TRISINDBIS CAPSID PROTEIN HAS THE CATALYTIC TRIAD OF THE SERINE PROTEINASE. THE RESIDUES ARE SER 215, HIS 141, AND ASP 163 IN THE WILD-TYPE. IN THIS MUTANT STRUCTURE, THE ACTIVE SITE SER 215 WAS MUTATED TO ALA TO PREVENT AUTO-CATALYTIC CLEAVAGE BETWEEN TRP 264 AND SER 265.H - 141

Clusters included in this Subclass
CLUSTER: AR.5.54