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5OGH

Structure of RNase A at high resolution (1.16 A) in complex with 3'-CMP and sulphate ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue C3P A 201
ChainResidue
AGLN11
AHOH351
AHIS12
ALYS41
AVAL43
AASN44
ATHR45
AHIS119
APHE120
AHOH332

site_idAC2
Number of Residues12
Detailsbinding site for residue C3P A 202
ChainResidue
ALYS1
AGLU2
AARG10
AASN34
AHIS105
AHOH333
AHOH342
AHOH346
AHOH348
AHOH358
AHOH359
AHOH366

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 203
ChainResidue
ATHR3
AALA4
ASER23
AHOH364
AHOH396
AHOH462

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 204
ChainResidue
AGLN55
ALYS61

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 205
ChainResidue
ANA209
AHOH337
AHOH437

site_idAC6
Number of Residues6
Detailsbinding site for residue CL A 206
ChainResidue
ASER50
ALEU51
AALA52
ANA209
AHOH452
AHOH459

site_idAC7
Number of Residues5
Detailsbinding site for residue CL A 207
ChainResidue
ASER16
AGLN55
ASER59
AHOH363
AHOH447

site_idAC8
Number of Residues4
Detailsbinding site for residue CL A 208
ChainResidue
AGLN74
ALYS98
AHIS105
AHOH445

site_idAC9
Number of Residues7
Detailsbinding site for residue NA A 209
ChainResidue
ASER15
ASER50
ALEU51
ASER59
ACL205
ACL206
AHOH334

site_idAD1
Number of Residues8
Detailsbinding site for residue NA A 210
ChainResidue
ALYS31
ASER32
AASN34
AHOH313
AHOH388
AHOH420
AHOH449
AHOH455

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF
ChainResidueDetails
ACYS40-PHE46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS119

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS7
AARG10
ALYS41
ALYS66
AARG85

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761
ChainResidueDetails
ALYS1
ALYS7
ALYS37
ALYS41

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553
ChainResidueDetails
AASN34

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 164
ChainResidueDetails
AHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS41electrostatic stabiliser, hydrogen bond donor
AHIS119hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APHE120electrostatic stabiliser, hydrogen bond donor
AASP121electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-07-31

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