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4M2Z

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004525molecular_functionribonuclease III activity
A0004530molecular_functiondeoxyribonuclease I activity
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0006396biological_processRNA processing
A0006397biological_processmRNA processing
A0008033biological_processtRNA processing
A0010468biological_processregulation of gene expression
A0016442cellular_componentRISC complex
A0016787molecular_functionhydrolase activity
A0030422biological_processsiRNA processing
A0031054biological_processpre-miRNA processing
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004525molecular_functionribonuclease III activity
B0004530molecular_functiondeoxyribonuclease I activity
B0005737cellular_componentcytoplasm
B0006364biological_processrRNA processing
B0006396biological_processRNA processing
B0006397biological_processmRNA processing
B0008033biological_processtRNA processing
B0010468biological_processregulation of gene expression
B0016442cellular_componentRISC complex
B0016787molecular_functionhydrolase activity
B0030422biological_processsiRNA processing
B0031054biological_processpre-miRNA processing
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP44
AGLU110
AHOH601
CC103
DG28
DHOH205

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
CG28
DC103
DHOH206
BASP44
BGLU110
BHOH402

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 101
ChainResidue
AHOH606
BGLU64
CA2
CHOH204
CHOH205

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 102
ChainResidue
CA2
CA3

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE C C 103
ChainResidue
AGLU40
APHE41
AASP44
AGLU110
AMG501
BGLU64
BSER68
BLYS71
CA2
CG26
CC27
CHOH204
DG28

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 101
ChainResidue
AGLU64
BHOH403
DA2
DHOH207
DHOH208

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG D 102
ChainResidue
DA2
DA3

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE C D 103
ChainResidue
AGLU64
ASER68
ALYS71
BGLU40
BPHE41
BASP44
BGLU110
BMG301
CG28
DA2
DG26
DC27
DHOH206
DHOH207

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

218853

PDB entries from 2024-04-24

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