7BBU: Human Prolyl-tRNA synthetase

Crystal Structure of human Prolyl-tRNA synthetase in complex with NCP26 and L-Proline. Determined by X-ray diffraction at 2.19 Å resolution. Released 12 Jan 2022.

Method
X-ray diffraction
Resolution
2.19 Å
Organism
Homo sapiens
Chains
1
Atoms
3,963
Mol. weight
59.66 kDa
Ligands
PRO, MU5, ZN
Released
12 Jan 2022

Explore 7BBU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7BBU contains 21 α-helices and 32 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 21 helices, 32 β-strands

ElementResiduesLengthSheet
α-helix1024-103411
β-strand1038-104031
β-strand1047-104931
α-helix1051-106919
β-strand1074-107522
β-strand1081-108223
α-helix1084-10885
β-strand1103-110753
β-strand1110-111893
α-helix11191
α-helix1123-113311
β-strand113614
α-helix1137-11393
β-strand1142-1151102
α-helix1157-11582
β-strand115915
β-strand116315
β-strand1166-1176112
α-helix1179-119517
α-helix1196-12005
β-strand1206-120942
α-helix12161
β-strand1221-122992
β-strand1234-1245122
α-helix1247-12526
β-strand1255-125734
β-strand1265-126734
α-helix12681
β-strand1269-127682
α-helix1278-128710
β-strand128916
β-strand129216
β-strand1304-130857
α-helix1318-133619
β-strand1341-134337
α-helix1351-136111
β-strand1365-136957
α-helix1371-13755
β-strand1378-138367
β-strand1389-139357
α-helix1397-142226
β-strand1424-142638
α-helix1430-14389
β-strand1442-144768
α-helix1451-146212
β-strand1477-148048
β-strand1481-148222
α-helix14931
β-strand149419
α-helix14951
β-strand150119
β-strand1504-150968
β-strand151112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bifunctional glutamate/proline--tRNA ligaseAprotein515Homo sapiensP07814 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7BBU_1 Bifunctional glutamate/proline--tRNA ligase (chains A)
SMSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIW
EAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIA
IRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFA
TMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQ
GGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPP
RVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNH
WELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRAS
EDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAK
SLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

Ligands and cofactors

IDNameFormulaCopies
PROProlineC5 H9 N O21
MU5~{N}-(2,3-dihydro-1~{H}-inden-2-yl)-3-(piperidin-1-ylcarbonylamino)pyrazine-2-c…C20 H23 N5 O21
ZNZinc ionZn1

Water and common crystallization additives (EDO, NO3, CL) are not listed.

Primary citation

Crystal Structure of human Prolyl-tRNA synthetase in complex with NCP26 and L-Proline. Johansson, C., Tye, M., Payne, N.C. et al. To be published.

Other PDB entries of the same protein (UniProt P07814 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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