2E2D

Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0031012	cellular_component	extracellular matrix
C	0002020	molecular_function	protease binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0008191	molecular_function	metalloendopeptidase inhibitor activity
C	0009725	biological_process	response to hormone
C	0030414	molecular_function	peptidase inhibitor activity
C	0031012	cellular_component	extracellular matrix
C	0034097	biological_process	response to cytokine
C	0046872	molecular_function	metal ion binding
C	0051045	biological_process	negative regulation of membrane protein ectodomain proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 500

Chain	Residue
A	HIS222
A	HIS226
A	HIS232
C	CYS1001

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	HIS172
A	ASP174
A	HIS187
A	HIS200

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 502

Chain	Residue
A	GLY180
A	SER182
A	LEU184
A	ASP202
A	GLU205
A	ASP179

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 503

Chain	Residue
A	ASP162
A	ASN194
A	GLY196
A	ASP198
A	HOH537
A	HOH551

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Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL

Chain	Residue	Details
A	VAL219-LEU228

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site_id	PS00288
Number of Residues	13
Details	TIMP Tissue inhibitors of metalloproteinases signature. CsCsPvHPQqaFC

Chain	Residue	Details
C	CYS1001-CYS1013

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	SITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:17196980, ECO:0007744|PDB:2E2D

Chain	Residue	Details
C	ASN1038
C	ALA1070
C	ARG1132
C	TRP1151

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305

Chain	Residue	Details
A	ASP128
A	ASP202
A	ASP203
A	GLU205
A	ASP162
A	ASP179
A	GLY180
A	SER182
A	LEU184
A	ASN194
A	GLY196
A	ASP198

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860

Chain	Residue	Details
A	HIS172
A	ASP174
A	HIS187
A	HIS200
A	HIS222
A	HIS226
A	HIS232
A	MET240

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151

Chain	Residue	Details
A	ASN117

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN152

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	GLU223
A	MET240

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	GLU223

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