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4M30

Crystal structure of RNASE III complexed with double-stranded RNA AND AMP (TYPE II CLEAVAGE)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0004519molecular_functionendonuclease activity
A0004525molecular_functionribonuclease III activity
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0006396biological_processRNA processing
A0006397biological_processmRNA processing
A0008033biological_processtRNA processing
A0010468biological_processregulation of gene expression
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0004519molecular_functionendonuclease activity
B0004525molecular_functionribonuclease III activity
B0005737cellular_componentcytoplasm
B0006364biological_processrRNA processing
B0006396biological_processRNA processing
B0006397biological_processmRNA processing
B0008033biological_processtRNA processing
B0010468biological_processregulation of gene expression
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP44
AGLU110
AMG502
AHOH601
CAMP103
DU28
DHOH201

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AMG501
AHOH602
AHOH603
CAMP103
AGLU40
AGLU110

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BASP44
BGLU110
BMG302
BHOH401
CU28
CHOH218
DAMP104

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 302
ChainResidue
BGLU40
BGLU110
BMG301
BHOH414
DAMP104

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 303
ChainResidue
AILE118
BVAL56
BGLN57
BLYS62

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 101
ChainResidue
AHOH621
AHOH622
AHOH623
CA2
CHOH215
CHOH216

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 102
ChainResidue
CA2
CA3
CHOH213
CHOH214
CHOH217

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMP C 103
ChainResidue
AGLU40
APHE41
AASP44
AGLU110
AMG501
AMG502
AHOH602
AHOH603
AHOH622
BSER68
BLYS71
CA2
CU26
CA27
DU28
DHOH201

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG D 101
ChainResidue
AGLU64
AHOH624
BHOH415
DA2
DHOH209
DHOH211
DHOH212

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 102
ChainResidue
DA2
DA3
DHOH204
DHOH210

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 103
ChainResidue
DC23

site_idBC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMP D 104
ChainResidue
AGLU64
ASER68
ALYS71
BGLU40
BPHE41
BASP44
BGLU110
BMG301
BMG302
BHOH414
CU28
CHOH218
DA2
DU26
DA27
DHOH211

Functional Information from PROSITE/UniProt
site_idPS00517
Number of Residues9
DetailsRNASE_3_1 Ribonuclease III family signature. ETLEFLGDA
ChainResidueDetails
AGLU37-ALA45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AASP44
BASP44

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305
ChainResidueDetails
AGLU110
BGLU110

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15016361, ECO:0000269|PubMed:18047582, ECO:0000305|PubMed:11738048, ECO:0007744|PDB:1JFZ, ECO:0007744|PDB:1RC5
ChainResidueDetails
AGLU40
AASP107
AGLU110
BGLU40
BASP107
BGLU110

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PDB entries from 2024-08-21

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