Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4M6R

Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006915biological_processapoptotic process
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0016829molecular_functionlyase activity
A0019509biological_processL-methionine salvage from methylthioadenosine
A0042802molecular_functionidentical protein binding
A0043066biological_processnegative regulation of apoptotic process
A0046570molecular_functionmethylthioribulose 1-phosphate dehydratase activity
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0070269biological_processpyroptotic inflammatory response
A0070372biological_processregulation of ERK1 and ERK2 cascade
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006915biological_processapoptotic process
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0009086biological_processmethionine biosynthetic process
B0016829molecular_functionlyase activity
B0019509biological_processL-methionine salvage from methylthioadenosine
B0042802molecular_functionidentical protein binding
B0043066biological_processnegative regulation of apoptotic process
B0046570molecular_functionmethylthioribulose 1-phosphate dehydratase activity
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B0070269biological_processpyroptotic inflammatory response
B0070372biological_processregulation of ERK1 and ERK2 cascade
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006915biological_processapoptotic process
C0008270molecular_functionzinc ion binding
C0008652biological_processamino acid biosynthetic process
C0009086biological_processmethionine biosynthetic process
C0016829molecular_functionlyase activity
C0019509biological_processL-methionine salvage from methylthioadenosine
C0042802molecular_functionidentical protein binding
C0043066biological_processnegative regulation of apoptotic process
C0046570molecular_functionmethylthioribulose 1-phosphate dehydratase activity
C0046872molecular_functionmetal ion binding
C0051289biological_processprotein homotetramerization
C0070269biological_processpyroptotic inflammatory response
C0070372biological_processregulation of ERK1 and ERK2 cascade
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006915biological_processapoptotic process
D0008270molecular_functionzinc ion binding
D0008652biological_processamino acid biosynthetic process
D0009086biological_processmethionine biosynthetic process
D0016829molecular_functionlyase activity
D0019509biological_processL-methionine salvage from methylthioadenosine
D0042802molecular_functionidentical protein binding
D0043066biological_processnegative regulation of apoptotic process
D0046570molecular_functionmethylthioribulose 1-phosphate dehydratase activity
D0046872molecular_functionmetal ion binding
D0051289biological_processprotein homotetramerization
D0070269biological_processpyroptotic inflammatory response
D0070372biological_processregulation of ERK1 and ERK2 cascade
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS115
AHIS117
AHIS195
AHOH425
AHOH481
DHOH446

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS195
BHOH492
BHOH494
AHOH486
BHIS115
BHIS117

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
BHOH424
CHIS115
CHIS117
CHIS195
CHOH443
CHOH448

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
CHOH418
DHIS115
DHIS117
DHIS195
DHOH415
DHOH462

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:24367089
ChainResidueDetails
AGLU139
BGLU139
CGLU139
DGLU139

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000305|PubMed:24367089
ChainResidueDetails
ACYS97
BCYS97
CCYS97
DCYS97

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000305|PubMed:24367089, ECO:0007744|PDB:4M6R
ChainResidueDetails
AHIS115
DHIS115
DHIS117
DHIS195
AHIS117
AHIS195
BHIS115
BHIS117
BHIS195
CHIS115
CHIS117
CHIS195

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER87
BSER87
CSER87
DSER87

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon