1SSG: Triosephosphate isomerase

Name: PDB 1SSG: Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
Published: 2004-08-24
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Aug 2004.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Gallus gallus
Chains: 2
Atoms: 3,905
Mol. weight: 54.15 kDa
Ligands: PGA
Released: 24 Aug 2004

Explore 1SSG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SSG contains 30 α-helices and 20 β-strands across 2 chains. 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: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
β-strand	7-11	5	1
β-strand	14	1	2
α-helix	18-30	13
β-strand	38-43	6	1
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	1
β-strand	72	1	3
α-helix	80-85	6
β-strand	90-93	4	1
α-helix	96-100	5
α-helix	106-118	13
β-strand	122-127	6	1
α-helix	131-135	5
α-helix	139-151	13
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	178-195	18
α-helix	198-203	6
β-strand	206-209	4	1
α-helix	217-222	6
β-strand	228-231	4	1
α-helix	233-236	4
α-helix	240-244	5

Chain B: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
β-strand	7-11	5	4
β-strand	14	1	3
α-helix	18-30	13
β-strand	38-43	6	4
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	4
β-strand	72	1	2
α-helix	80-85	6
β-strand	90-93	4	4
α-helix	96-100	5
α-helix	106-118	13
β-strand	122-127	6	4
α-helix	131-136	6
α-helix	139-151	13
β-strand	160-164	5	4
α-helix	167-169	3
α-helix	178-195	18
α-helix	198-203	6
β-strand	205-209	5	4
α-helix	217-222	6
β-strand	228-231	4	4
α-helix	233-236	4
α-helix	240-244	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Triosephosphate isomerase	A, B	protein	247	Gallus gallus	P00940 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1SSG_1 Triosephosphate isomerase (chains A, B)
APRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGV
AAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGYSLTPQQA
QEVHEKLRGWLKSHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH

Ligands and cofactors

ID	Name	Formula	Copies
PGA	2-phosphoglycolic acid	C2 H5 O6 P	2

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase. Kursula, I., Salin, M., Sun, J. et al. Protein Eng Des Sel (2004) 17:375-382. DOI 10.1093/protein/gzh048 · PubMed

Other PDB entries of the same protein (UniProt P00940 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4P61 1.34 Å, Chicken triosephosphate isomerase with LOOP6 mutations, V167P and W168E.
1SW0 1.71 Å, Triosephosphate isomerase from Gallus gallus, loop 6 hinge mutant K174L, T175W
1TPH 1.8 Å, 1.8 Å crystal structure of wild type chicken triosephosphate…
1TPB 1.9 Å, Offset of a catalytic lesion by a bound water soluble
1TPC 1.9 Å, Offset of a catalytic lesion by a bound water soluble
1TPU 1.9 Å, S96P change is a second-site suppressor for H95N sluggish mutant triosephosphate isomerase
1TPV 1.9 Å, S96P change is a second-site suppressor for H95N sluggish mutant triosephosphate isomerase
1TPW 1.9 Å, Triosephosphate isomerase drinks water to keep healthy
1SW3 2.03 Å, Triosephosphate isomerase from Gallus gallus, loop 6 mutant T175V
1SPQ 2.16 Å, Understanding protein lids: Structural analysis of active hinge mutants in…
1SW7 2.22 Å, Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S
1TIM 2.5 Å, Structure of triose phosphate isomerase from chicken muscle

Browse structure collections

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