Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Q3A

Crystal structure of the catalytic domain of human matrix metalloproteinase 10

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
B	0004222	molecular_function	metalloendopeptidase activity
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0031012	cellular_component	extracellular matrix
C	0004222	molecular_function	metalloendopeptidase activity
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0031012	cellular_component	extracellular matrix

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 464

Chain	Residue
A	HIS217
A	HIS221
A	HIS227
A	NGH480

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 465

Chain	Residue
A	HIS167
A	ASP169
A	HIS182
A	HIS195

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 466

Chain	Residue
A	GLY175
A	GLY177
A	SER179
A	ASP197
A	GLU200
A	ASP174

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 467

Chain	Residue
A	ASP157
A	GLY189
A	TYR191
A	ASP193

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 468

Chain	Residue
A	ASP123
A	ASP198
A	GLU200
A	HOH564
A	HOH597

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 469

Chain	Residue
B	HIS217
B	HIS221
B	HIS227
B	NGH479

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 470

Chain	Residue
B	HIS167
B	ASP169
B	HIS182
B	HIS195

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 471

Chain	Residue
B	ASP174
B	GLY175
B	GLY177
B	SER179
B	ASP197
B	GLU200

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 472

Chain	Residue
B	ASP157
B	GLY189
B	TYR191
B	ASP193
B	HOH513

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 473

Chain	Residue
B	ASP123
B	ASP198
B	GLU200
B	HOH482
B	HOH500

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 474

Chain	Residue
C	HIS217
C	HIS221
C	HIS227
C	NGH481
C	HOH491

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 475

Chain	Residue
C	HIS167
C	ASP169
C	HIS182
C	HIS195

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 476

Chain	Residue
C	ASP174
C	GLY175
C	GLY177
C	SER179
C	ASP197
C	GLU200

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 477

Chain	Residue
C	ASP157
C	GLY189
C	TYR191
C	ASP193
C	HOH498

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA C 478

Chain	Residue
C	ASP123
C	ASP198
C	GLU200

site_id	BC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NGH B 479

Chain	Residue
B	SER179
B	LEU180
B	ALA181
B	LEU213
B	HIS217
B	GLU218
B	HIS221
B	HIS227
B	PRO237
B	TYR239
B	ZN469
B	HOH583
C	HIS178

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NGH A 480

Chain	Residue
A	HIS178
A	SER179
A	LEU180
A	ALA181
A	LEU213
A	HIS217
A	GLU218
A	HIS221
A	HIS227
A	PRO237
A	SER241
A	ZN464
A	HOH485
A	HOH612
B	HIS178

site_id	BC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NGH C 481

Chain	Residue
B	PHE242
B	HOH499
B	HOH535
B	HOH605
C	SER179
C	LEU180
C	ALA181
C	HIS217
C	GLU218
C	HIS221
C	HIS227
C	LEU234
C	LEU238
C	TYR239
C	ZN474
C	HOH491
C	HOH504
C	HOH517
C	HOH520
C	HOH544
B	ASN240

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL214-LEU223

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000255\|PROSITE-ProRule:PRU10095, ECO:0000269\|PubMed:15095982

Chain	Residue	Details
A	GLU218
B	GLU218
C	GLU218

site_id	SWS_FT_FI2
Number of Residues	21
Details	BINDING:

Chain	Residue	Details
A	HIS167
B	HIS182
B	HIS195
B	HIS217
B	HIS221
B	HIS227
C	HIS167
C	ASP169
C	HIS182
C	HIS195
C	HIS217
A	ASP169
C	HIS221
C	HIS227
A	HIS182
A	HIS195
A	HIS217
A	HIS221
A	HIS227
B	HIS167
B	ASP169

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU218
A	MET235

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
B	GLU218
B	MET235

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	GLU218
C	MET235

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	GLU218

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
B	GLU218

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	GLU218

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)