1BZQ
COMPLEX OF A DROMEDARY SINGLE-DOMAIN VHH ANTIBODY FRAGMENT WITH RNASE A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004522 | molecular_function | ribonuclease A activity |
A | 0004540 | molecular_function | RNA nuclease activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0016829 | molecular_function | lyase activity |
A | 0050830 | biological_process | defense response to Gram-positive bacterium |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004519 | molecular_function | endonuclease activity |
B | 0004522 | molecular_function | ribonuclease A activity |
B | 0004540 | molecular_function | RNA nuclease activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0016829 | molecular_function | lyase activity |
B | 0050830 | biological_process | defense response to Gram-positive bacterium |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0004519 | molecular_function | endonuclease activity |
C | 0004522 | molecular_function | ribonuclease A activity |
C | 0004540 | molecular_function | RNA nuclease activity |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0016829 | molecular_function | lyase activity |
C | 0050830 | biological_process | defense response to Gram-positive bacterium |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0004519 | molecular_function | endonuclease activity |
D | 0004522 | molecular_function | ribonuclease A activity |
D | 0004540 | molecular_function | RNA nuclease activity |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0016829 | molecular_function | lyase activity |
D | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
Chain | Residue |
A | LYS7 |
A | GLN11 |
A | HIS12 |
A | HIS119 |
A | PHE120 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 2002 |
Chain | Residue |
B | PHE320 |
B | GLN211 |
B | HIS212 |
B | LYS241 |
B | HIS319 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 2003 |
Chain | Residue |
C | GLN411 |
C | HIS412 |
C | HIS519 |
C | PHE520 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 D 2004 |
Chain | Residue |
D | GLN611 |
D | HIS612 |
D | LYS641 |
D | HIS719 |
D | PHE720 |
Functional Information from PROSITE/UniProt
site_id | PS00127 |
Number of Residues | 7 |
Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF |
Chain | Residue | Details |
A | CYS40-PHE46 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS12 | |
B | HIS212 | |
C | HIS412 | |
D | HIS612 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS119 | |
B | HIS319 | |
C | HIS519 | |
D | HIS719 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS7 | |
B | ARG285 | |
C | LYS407 | |
C | ARG410 | |
C | LYS441 | |
C | LYS466 | |
C | ARG485 | |
D | LYS607 | |
D | ARG610 | |
D | LYS641 | |
D | LYS666 | |
A | ARG10 | |
D | ARG685 | |
A | LYS41 | |
A | LYS66 | |
A | ARG85 | |
B | LYS207 | |
B | ARG210 | |
B | LYS241 | |
B | LYS266 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
Chain | Residue | Details |
A | LYS1 | |
C | LYS407 | |
C | LYS437 | |
C | LYS441 | |
D | LYS601 | |
D | LYS607 | |
D | LYS637 | |
D | LYS641 | |
A | LYS7 | |
A | LYS37 | |
A | LYS41 | |
B | LYS201 | |
B | LYS207 | |
B | LYS237 | |
B | LYS241 | |
C | LYS401 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
Chain | Residue | Details |
A | ASN34 | |
B | ASN234 | |
C | ASN434 | |
D | ASN634 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
A | PHE120 | |
A | HIS119 | |
A | HIS12 | |
A | LYS41 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
B | HIS212 | |
B | HIS319 | |
B | PHE320 | |
B | LYS241 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
C | LYS441 | |
C | PHE520 | |
C | HIS519 | |
C | HIS412 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
D | LYS641 | |
D | HIS719 | |
D | HIS612 | |
D | PHE720 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
A | HIS119 | |
A | HIS12 | |
A | LYS41 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
B | HIS212 | |
B | HIS319 | |
B | LYS241 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
C | LYS441 | |
C | HIS519 | |
C | HIS412 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
D | LYS641 | |
D | HIS719 | |
D | HIS612 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 164 |
Chain | Residue | Details |
A | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LYS41 | electrostatic stabiliser, hydrogen bond donor |
A | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | PHE120 | electrostatic stabiliser, hydrogen bond donor |
A | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 164 |
Chain | Residue | Details |
B | HIS212 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | LYS241 | electrostatic stabiliser, hydrogen bond donor |
B | HIS319 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | PHE320 | electrostatic stabiliser, hydrogen bond donor |
B | ASP321 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 164 |
Chain | Residue | Details |
C | HIS412 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | LYS441 | electrostatic stabiliser, hydrogen bond donor |
C | HIS519 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | PHE520 | electrostatic stabiliser, hydrogen bond donor |
C | ASP521 | electrostatic stabiliser, hydrogen bond acceptor |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 164 |
Chain | Residue | Details |
D | HIS612 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | LYS641 | electrostatic stabiliser, hydrogen bond donor |
D | HIS719 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | PHE720 | electrostatic stabiliser, hydrogen bond donor |
D | ASP721 | electrostatic stabiliser, hydrogen bond acceptor |