1ANC: Anionic trypsin

Anionic trypsin mutant with ser 214 replaced by lys. Determined by X-ray diffraction at 2.2 Å resolution. Released 1 Apr 1997.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Rattus rattus
Chains: 1
Atoms: 1,846
Mol. weight: 24.14 kDa
Ligands: BEN, CA
Released: 1 Apr 1997

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

Secondary structure: helices and β-sheets

1ANC contains 8 α-helices and 20 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: 8 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-34	5	3
β-strand	40-48	9	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	64-66	4	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	95	1	5
β-strand	100	1	5
β-strand	104-108	5	3
β-strand	122	1	2
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	2
β-strand	154	1	4
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	204-215	8	2
β-strand	226-230	5	2
α-helix	231-233	3
α-helix	235-243	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anionic trypsin	A	protein	223	Rattus rattus	P00763 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ANC_1 ANIONIC TRYPSIN (chains A)
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEG
NEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISG
WGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGP
VVCNGELQGIVKWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN

Ligands and cofactors

ID	Name	Formula	Copies
BEN	Benzamidine	C7 H8 N2	2
CA	Calcium ion	Ca	1

Primary citation

Perturbing the polar environment of Asp102 in trypsin: consequences of replacing conserved Ser214. McGrath, M.E., Vasquez, J.R., Craik, C.S. et al. Biochemistry (1992) 31:3059-3064. DOI 10.1021/bi00127a005 · PubMed

Other PDB entries of the same protein (UniProt P00763 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FP7 1.46 Å, Anionic trypsin variant S195A in complex with bovine pancreatic trypsin inhibitor (BPTI)…
3FP8 1.46 Å, Anionic trypsin variant S195A in complex with bovine pancreatic trypsin inhibitor (BPTI)…
3FP6 1.49 Å, Anionic trypsin in complex with bovine pancreatic trypsin inhibitor (BPTI) determined to…
1F7Z 1.55 Å, Rat trypsinogen K15A complexed with bovine pancreatic trypsin inhibitor
1DPO 1.59 Å, Structure of rat trypsin
1J16 1.6 Å, Benzamidine in complex with rat trypsin mutant X99/175/190RT
1F5R 1.65 Å, Rat trypsinogen mutant complexed with bovine pancreatic trypsin inhibitor
1FY8 1.7 Å, Crystal structure of the DELTAILE16VAL17 rat anionic trypsinogen-bpti complex
1YKT 1.7 Å, Trypsin/Bpti complex mutant
1YLC 1.7 Å, Trypsin/BPTI complex mutant
1YLD 1.7 Å, Trypsin/BPTI complex mutant
3TGK 1.7 Å, Trypsinogen mutant D194N and deletion of ile 16-val 17 complexed with bovine pancreatic…

Browse structure collections

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