1AZZ: Fiddler crab collagenase complexed to ecotin

Fiddler crab collagenase complexed to ecotin. Determined by X-ray diffraction at 2.3 Å resolution. Released 25 Feb 1998.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Celuca pugilator, Escherichia coli
Chains: 4
Atoms: 5,527
Mol. weight: 79.28 kDa
Released: 25 Feb 1998

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

Secondary structure: helices and β-sheets

1AZZ contains 23 α-helices and 79 β-strands across 4 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: 6 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-35	6	3
β-strand	40-48	9	3
β-strand	51-54	4	3
α-helix	56-59	4
β-strand	63-68	5	3
β-strand	72	1	4
β-strand	81-85	5	3
β-strand	88-90	3	3
β-strand	95	1	5
β-strand	100	1	5
β-strand	104-107	4	3
β-strand	122	1	6
α-helix	123-124	2
β-strand	135-136	2	7
β-strand	137-138	2	6
β-strand	139-140	2	2
β-strand	154	1	4
β-strand	156-157	2	2
β-strand	160-161	2	7
β-strand	162-163	2	6
α-helix	165-172	8
β-strand	180-183	4	6
β-strand	189	1	1
β-strand	198-201	4	6
β-strand	204-217	10	6
β-strand	226-230	5	6
α-helix	232-234	3
α-helix	235-242	8

Chain B: 7 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	8
β-strand	20-21	2	9
α-helix	22-23	2
β-strand	30-35	6	10
β-strand	40-48	9	10
β-strand	51-54	4	10
α-helix	56-59	4
β-strand	63-68	5	10
β-strand	72	1	11
β-strand	81-85	5	10
β-strand	87-90	4	10
β-strand	95	1	12
β-strand	100	1	12
β-strand	104-107	4	10
α-helix	111-113	3
β-strand	122	1	13
α-helix	123-124	2
β-strand	135-136	2	14
β-strand	137-138	2	13
β-strand	139-140	2	9
β-strand	154	1	11
β-strand	156-157	2	9
β-strand	160-161	2	14
β-strand	162-163	2	13
α-helix	165-172	8
β-strand	180-183	4	13
β-strand	189	1	8
β-strand	198-201	4	13
β-strand	204-217	10	13
β-strand	226-230	5	13
α-helix	231-234	4
α-helix	235-242	8

Chain C: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	7-9	3
α-helix	13-16	4
β-strand	20-25	6	15
α-helix	27-29	3
β-strand	36-48	13	16
β-strand	53-54	2	6
β-strand	55-56	2	17
β-strand	58-64	7	15
β-strand	69-75	7	15
β-strand	81-83	3	6
α-helix	85	1
β-strand	86	1	3
α-helix	87-88	2
β-strand	93-98	6	16
β-strand	99-100	2	17
β-strand	106-108	3	16
β-strand	115-120	6	15
β-strand	124-132	9	16
β-strand	137-138	2	16
β-strand	140-141	2	18

Chain D: 5 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	7-9	3
α-helix	13-16	4
β-strand	20-25	6	18
α-helix	27-29	3
β-strand	36-48	13	16
β-strand	53-54	2	13
β-strand	55-56	2	19
β-strand	58-64	7	18
β-strand	69-75	7	18
β-strand	81-83	3	13
α-helix	85	1
β-strand	86	1	10
α-helix	87	1
β-strand	93-98	6	16
β-strand	99-100	2	19
β-strand	106-108	3	16
β-strand	115-120	6	18
β-strand	124-138	15	16
β-strand	140-141	2	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Collagenase	A, B	protein	226	Celuca pugilator	P00771 (AlphaFold model)
Ecotin	C, D	protein	142	Escherichia coli	P23827 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1AZZ_1 COLLAGENASE (chains A, B)
IVGGVEAVPNSWPHQAALFIDDMYFCGGSLISPEWILTAAHCMDGAGFVDVVLGAHNIRE
DEATQVTIQSTDFTVHENYNSFVISNDIAVIRLPVPVTLTAAIATVGLPSTDVGVGTVVT
PTGWGLPSDSALGISDVLRQVDVPIMSNADCDAVYGIVTDGNICIDSTGGKGTCNGDSGG
PLNYNGLTYGITSFGAAAGCEAGYPDAFTRVTYFLDWIQTQTGITP

Sequence of entity 2 (C, D), FASTA

>1AZZ_2 ECOTIN (chains C, D)
AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE
NKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP
DNVDVKYRVWKAEEKIDNAVVR

Primary citation

Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Perona, J.J., Tsu, C.A., Craik, C.S. et al. Biochemistry (1997) 36:5381-5392. DOI 10.1021/bi9617522 · PubMed

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