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4QMG

The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
B0003676molecular_functionnucleic acid binding
B0004518molecular_functionnuclease activity
C0003676molecular_functionnucleic acid binding
C0004518molecular_functionnuclease activity
D0003676molecular_functionnucleic acid binding
D0004518molecular_functionnuclease activity
E0003676molecular_functionnucleic acid binding
E0004518molecular_functionnuclease activity
F0043066biological_processnegative regulation of apoptotic process
F0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
F0045766biological_processpositive regulation of angiogenesis
G0043066biological_processnegative regulation of apoptotic process
G0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
G0045766biological_processpositive regulation of angiogenesis
H0043066biological_processnegative regulation of apoptotic process
H0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
H0045766biological_processpositive regulation of angiogenesis
I0043066biological_processnegative regulation of apoptotic process
I0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
I0045766biological_processpositive regulation of angiogenesis
J0043066biological_processnegative regulation of apoptotic process
J0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
J0045766biological_processpositive regulation of angiogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
ASER170
AHIS171
AILE173
AASP175

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS A 402
ChainResidue
AMSE163
ASER165
AGLY167

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
BARG174
BGLU200

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS B 402
ChainResidue
BMSE163
BSER165
BGLY167

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
BHIS201
BARG203
BARG209

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BHIS201
BVAL202
BLYS249
BGLU253

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 401
ChainResidue
CARG83
CARG174
CGLU200

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS C 402
ChainResidue
CMSE163
CSER165
CGLY167

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 401
ChainResidue
DARG83
DARG174
DGLU200

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS D 402
ChainResidue
DMSE163
DSER165
DGLY167

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 403
ChainResidue
DHIS201
DARG203
DARG209

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 401
ChainResidue
ELEU59
EALA60
EARG83
EARG174
EGLU200

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS E 402
ChainResidue
EMSE163
ESER165
EGLY167

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL E 403
ChainResidue
EHIS201
EARG203
EARG209

Functional Information from PROSITE/UniProt
site_idPS01284
Number of Residues11
DetailsTNASE_2 Thermonuclease family signature 2. TPQGReYGmIY
ChainResidueDetails
ATHR103-TYR113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR103
ETHR240
ATHR240
BTHR103
BTHR240
CTHR103
CTHR240
DTHR103
DTHR240
ETHR103

site_idSWS_FT_FI2
Number of Residues5
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS193
BLYS193
CLYS193
DLYS193
ELYS193

224004

PDB entries from 2024-08-21

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