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1C8T

HUMAN STROMELYSIN-1 (E202Q) CATALYTIC DOMAIN COMPLEXED WITH RO-26-2812

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 260
ChainResidue
BHIS201
BHIS205
BHIS211
BTR1265

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 261
ChainResidue
BHIS151
BASP153
BHIS166
BHIS179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 262
ChainResidue
BGLY159
BGLY161
BVAL163
BASP181
BGLU184
BASP158

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 263
ChainResidue
BHOH53
BASP141
BGLY173
BASN175
BASP177

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 264
ChainResidue
BHOH42
BASP107
BASP182
BGLU184
BGLN185

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 260
ChainResidue
AHIS201
AHIS205
AHIS211
ATR1265

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 261
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 262
ChainResidue
AASP158
AGLY159
AGLY161
AVAL163
AASP181
AGLU184

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 263
ChainResidue
AASP141
AGLY173
AASN175
AASP177

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 264
ChainResidue
AASP107
AASP182
AGLU184

site_idBC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE TR1 A 265
ChainResidue
AASN162
AVAL163
ALEU164
AALA165
ALEU197
AHIS201
AGLN202
AHIS211
AALA217
ALEU218
ATYR220
APRO221
ALEU222
ATYR223
AHIS224
AZN260
BPRO87
BALA213
BTHR215
BTYR220

site_idBC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TR1 B 265
ChainResidue
AHOH41
APRO87
ATHR215
AGLU216
BASN162
BLEU164
BVAL198
BHIS201
BGLN202
BHIS205
BHIS211
BALA217
BLEU218
BTYR220
BPRO221
BLEU222
BTYR223
BHIS224
BZN260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLN202
BGLN202

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING:
ChainResidueDetails
AASP158
AGLY159
AGLY161
AVAL163
AHIS166
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
BASP107
BASP141
BHIS151
BASP153
BASP158
BGLY159
BGLY161
BVAL163
BHIS166
BGLY173
BASN175
BASP177
BHIS179
BASP181
BASP182
BGLU184
AASP107
AASP141
AHIS151
AASP153

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8740360
ChainResidueDetails
BHIS205
BHIS211
AHIS201
AHIS205
AHIS211
BHIS201

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
AHIS201metal ligand
AGLN202proton acceptor, proton donor
AHIS205metal ligand
AHIS211metal ligand

site_idMCSA2
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
BHIS201metal ligand
BGLN202proton acceptor, proton donor
BHIS205metal ligand
BHIS211metal ligand

218500

PDB entries from 2024-04-17

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