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2P6Z

Enzymatic and Structural Characterisation of Amphinase, a Novel Cytotoxic Ribonuclease from Rana pipiens Oocytes

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0050830biological_processdefense response to Gram-positive bacterium
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0004540molecular_functionRNA nuclease activity
B0005576cellular_componentextracellular region
B0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 401
ChainResidue
BILE44
BCIT502
BHOH514
BHOH531
BHOH643

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AGLN73
ATHR93
AHOH629
AHOH647

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 403
ChainResidue
BTHR71
BCIT503
BHOH526
BHOH541
BHOH567

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CIT A 501
ChainResidue
ALYS14
AHIS15
AASN45
ATHR46
AHIS107
APHE108
AHOH504
AHOH518
AHOH529
AHOH537
AHOH547
AHOH557
BCIT502
BHOH534

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CIT B 502
ChainResidue
ACIT501
AHOH518
AHOH544
BLYS14
BHIS15
BASN45
BTHR46
BPHE108
BNA401
BHOH506
BHOH534
BHOH544
BHOH550
BHOH570

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT B 503
ChainResidue
BGLU57
BARG60
BSER70
BTHR71
BGLN72
BNA403
BHOH541
BHOH611

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpiNTF
ChainResidueDetails
ACYS41-PHE47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P11916
ChainResidueDetails
AHIS15
BHIS15

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P11916
ChainResidueDetails
AHIS107
BHIS107

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11916
ChainResidueDetails
ALYS42
BLYS42

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17560606
ChainResidueDetails
AASN27
BASN27

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN67
AASN91
BASN67
BASN91

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
AHIS107
AHIS15
ALYS42

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
BHIS107
BHIS15
BLYS42

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
AHIS107
AHIS15
ALYS42
APHE108

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
BHIS107
BHIS15
BLYS42
BPHE108

227561

PDB entries from 2024-11-20

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