1GXD: ProMMP-2/TIMP-2 complex

proMMP-2/TIMP-2 complex. Determined by X-ray diffraction at 3.1 Å resolution. Released 9 Jul 2002.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 12,945
Mol. weight: 186.09 kDa
Ligands: CA, ZN
Released: 9 Jul 2002

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

Secondary structure: helices and β-sheets

1GXD contains 52 α-helices and 136 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: 14 helices, 54 β-strands

Element	Residues	Length	Sheet
α-helix	18-23	6
α-helix	45-50	6
β-strand	72	1	1
β-strand	94-97	4	2
β-strand	98-99	2	3
α-helix	108-123	16
β-strand	129-132	4	2
β-strand	141-145	5	3
β-strand	161	1	1
β-strand	163-165	3	3
β-strand	176-179	4	3
β-strand	184-185	2	4
β-strand	193	1	5
α-helix	197-199	3
β-strand	203	1	5
α-helix	204	1
β-strand	208-210	3	6
β-strand	213-215	3	6
β-strand	219	1	7
β-strand	229-231	3	7
β-strand	235	1	6
α-helix	236-239	4
β-strand	242-244	3	7
α-helix	245-246	2
β-strand	253	1	8
β-strand	266-267	2	9
β-strand	272-273	2	9
β-strand	277	1	8
β-strand	287-289	3	8
β-strand	293	1	9
α-helix	294-297	4
β-strand	300-302	3	8
β-strand	311	1	10
β-strand	324-326	3	11
β-strand	329-331	3	11
β-strand	335	1	10
β-strand	345-347	3	10
β-strand	351	1	11
α-helix	352-355	4
β-strand	358-360	3	10
β-strand	366-367	2	4
α-helix	368-380	13
β-strand	395	1	1
α-helix	406-415	10
β-strand	449-451	3	12
β-strand	456-458	3	12
β-strand	463-464	2	13
β-strand	465	1	12
β-strand	478-479	2	13
α-helix	480-482	3
β-strand	494-497	4	14
β-strand	502-507	6	14
β-strand	510-515	6	14
β-strand	518-519	2	14
α-helix	520	1
β-strand	525-526	2	14
β-strand	541-544	4	15
β-strand	551-555	5	15
β-strand	558-559	2	15
β-strand	562	1	15
β-strand	575-576	2	15
β-strand	590-593	4	16
β-strand	599	1	17
β-strand	600-604	5	16
β-strand	607-609	3	16
β-strand	612	1	17
β-strand	621-623	3	16
α-helix	624-627	4

Chain B: 21 helices, 53 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	18
α-helix	17-26	10
α-helix	38-41	4
α-helix	47-52	6
α-helix	61-69	9
β-strand	72	1	19
β-strand	94-99	6	20
α-helix	108-123	16
β-strand	129-132	4	20
β-strand	140-145	6	20
β-strand	161	1	19
β-strand	163-165	3	20
α-helix	166-167	2
β-strand	176-179	4	20
β-strand	184-185	2	21
β-strand	193	1	22
β-strand	203	1	22
α-helix	204	1
β-strand	208-210	3	23
β-strand	213-215	3	23
β-strand	219	1	24
β-strand	229-231	3	24
β-strand	235	1	23
α-helix	236-239	4
β-strand	242-244	3	24
α-helix	245-246	2
β-strand	247	1	25
β-strand	251	1	25
β-strand	253	1	26
α-helix	261-263	3
β-strand	266-267	2	9
β-strand	272-273	2	9
β-strand	277	1	26
β-strand	287-289	3	26
β-strand	293	1	9
α-helix	294-297	4
β-strand	300-302	3	26
β-strand	311	1	27
β-strand	324-326	3	28
β-strand	329-331	3	28
β-strand	335	1	27
β-strand	338	1	18
β-strand	345-347	3	27
β-strand	351	1	28
α-helix	352-355	4
β-strand	358-360	3	27
β-strand	366-367	2	21
α-helix	368-379	12
β-strand	395	1	19
α-helix	406-416	11
β-strand	449-452	4	29
β-strand	455-460	6	29
β-strand	463-467	5	29
α-helix	473-474	2
α-helix	480-482	3
α-helix	488	1
β-strand	493-496	4	30
β-strand	503-507	5	30
β-strand	510-515	6	30
β-strand	518-519	2	30
α-helix	520	1
β-strand	525-526	2	30
β-strand	541	1	31
β-strand	544	1	31
β-strand	551-554	4	31
β-strand	559-562	4	31
α-helix	568-570	3
α-helix	577-579	3
β-strand	590-591	2	32
β-strand	596	1	32
β-strand	599-604	6	32
β-strand	607-612	6	32
β-strand	621-623	3	32
α-helix	624-627	4

Chain C: 9 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	8-14	7
β-strand	17-19	3	33
β-strand	21	1	34
β-strand	23-26	4	35
β-strand	34	1	36
β-strand	37	1	36
β-strand	43-47	5	35
β-strand	52-54	3	33
β-strand	62-65	4	35
α-helix	69-72	4
β-strand	78	1	35
β-strand	84	1	34
α-helix	88	1
β-strand	89-91	3	35
β-strand	95-97	3	35
β-strand	106	1	34
α-helix	112-116	5
α-helix	117-121	5
α-helix	122-124	3
β-strand	131-132	2	37
β-strand	138	1	16
β-strand	147-148	2	37
α-helix	150-153	4
α-helix	160-163	4
β-strand	168-169	2	38
β-strand	175-176	2	38

Chain D: 8 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	8-14	7
β-strand	17-21	5	39
β-strand	26-34	9	40
β-strand	38-46	9	40
β-strand	52	1	39
β-strand	62-65	4	40
α-helix	69-71	3
α-helix	78-80	3
β-strand	84-88	5	39
β-strand	89-90	2	40
β-strand	95-97	3	40
β-strand	105-106	2	39
α-helix	112-115	4
α-helix	123-125	3
α-helix	150-152	3
β-strand	168-169	2	41
α-helix	170	1
β-strand	175-176	2	41

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
72 kda type IV collagenase	A, B	protein	631	HOMO SAPIENS	P08253 (AlphaFold model)
Metalloproteinase inhibitor 2	C, D	protein	194	HOMO SAPIENS	P16035 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1GXD_1 72 KDA TYPE IV COLLAGENASE (chains A, B)
APSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDL
DQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQ
VWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDD
DELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDG
KYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKY
GFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGF
CPDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASP
DIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLV
ATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVD
AAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHS
YFFKGAYYLKLENQSLKSVKFGSIKSDWLGC

Sequence of entity 2 (C, D), FASTA

>1GXD_2 METALLOPROTEINASE INHIBITOR 2 (chains C, D)
CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDI
EFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNH
RYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRG
AAPPKQEFLDIEDP

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
ZN	Zinc ion	Zn	4

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

Primary citation

Structural Insight Into the Complex Formation of Latent Matrix Metalloproteinase 2 with Tissue Inhibitor of Metalloproteinase 2. Morgunova, E., Tuuttila, A., Bergmann, U. et al. Proc Natl Acad Sci U S A (2002) 99:7414. DOI 10.1073/PNAS.102185399 · PubMed

Other PDB entries of the same protein (UniProt P08253 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3AYU 2.0 Å, Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide…
7XJO 2.0 Å, Crystal structure of human MMP-2 catalytic domain in complex with inhibitor
1GEN 2.15 Å, C-terminal domain of gelatinase a
8H78 2.4 Å, Crystal structure of human MMP-2 catalytic domain in complex with inhibitor
1RTG 2.6 Å, C-terminal domain (haemopexin-like domain) of human matrix metalloproteinase-2
1EAK 2.66 Å, Catalytic domain of proMMP-2 E404Q mutant
1CK7 2.8 Å, Gelatinase a (full-length)
1QIB 2.8 Å, Crystal structure of gelatinase a catalytic domain
7XGJ 2.8 Å, Crystal structure of human MMP-2 catalytic domain in complex with inhibitor
1CXW The second type II module from human matrix metalloproteinase 2
1HOV Solution structure of a catalytic domain of mmp-2 complexed with sc-74020
1J7M The Third Fibronectin Type II Module from Human Matrix Metalloproteinase 2

Browse structure collections

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