Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ZAE

Crystal structure of protein Ph1601p in complex with protein Ph1771p of archaeal ribonuclease P from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0001682biological_processtRNA 5'-leader removal
A0003723molecular_functionRNA binding
A0004519molecular_functionendonuclease activity
A0004526molecular_functionribonuclease P activity
A0005737cellular_componentcytoplasm
A0006396biological_processRNA processing
A0008033biological_processtRNA processing
A0030677cellular_componentribonuclease P complex
B0001682biological_processtRNA 5'-leader removal
B0004519molecular_functionendonuclease activity
B0004526molecular_functionribonuclease P activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006396biological_processRNA processing
B0008033biological_processtRNA processing
B0008270molecular_functionzinc ion binding
B0030677cellular_componentribonuclease P complex
B0046872molecular_functionmetal ion binding
B1902555cellular_componentendoribonuclease complex
B1990904cellular_componentribonucleoprotein complex
C0001682biological_processtRNA 5'-leader removal
C0003723molecular_functionRNA binding
C0004519molecular_functionendonuclease activity
C0004526molecular_functionribonuclease P activity
C0005737cellular_componentcytoplasm
C0006396biological_processRNA processing
C0008033biological_processtRNA processing
C0030677cellular_componentribonuclease P complex
D0001682biological_processtRNA 5'-leader removal
D0004519molecular_functionendonuclease activity
D0004526molecular_functionribonuclease P activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006396biological_processRNA processing
D0008033biological_processtRNA processing
D0008270molecular_functionzinc ion binding
D0030677cellular_componentribonuclease P complex
D0046872molecular_functionmetal ion binding
D1902555cellular_componentendoribonuclease complex
D1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 121
ChainResidue
BCYS68
BCYS71
BCYS97
BCYS100

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 121
ChainResidue
DCYS68
DCYS71
DCYS97
DCYS100

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 128
ChainResidue
AARG26
ATHR27
ATRP28
AHOH176
CTRP28
AGLY25

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NO3 D 122
ChainResidue
BPRO77
DARG82

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 D 123
ChainResidue
CARG54
CGLY65
CGLU67
CHOH161
DMET90
DPRO91
DHIS92
DHOH148

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 C 128
ChainResidue
BARG89
CGLN17
CSER19

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A 130
ChainResidue
AHIS60
AASP91
AVAL92

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 C 129
ChainResidue
ATRP28
CGLY25
CARG26
CTHR27
CTRP28
CHOH160
DLYS88

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 C 130
ChainResidue
CTHR74
CARG75
CARG115
CPRO116
CHOH155
DARG43

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 122
ChainResidue
BPRO77
BGLY78
BARG82
BVAL83
BARG84
DARG82
DTHR96
DHOH192

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 131
ChainResidue
ASER58
ATHR59
AVAL92
AILE94

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 123
ChainResidue
BTYR102
BILE103
CPRO61

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 124
ChainResidue
DTYR102
DILE103
DHOH171

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 132
ChainResidue
AHIS60
AALA62

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
BCYS68
BCYS71
BCYS97
BCYS100
DCYS68
DCYS71
DCYS97
DCYS100

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon