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

3RMJ

Crystal structure of truncated alpha-Isopropylmalate Synthase from Neisseria meningitidis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0019752biological_processcarboxylic acid metabolic process
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0003824molecular_functioncatalytic activity
B0019752biological_processcarboxylic acid metabolic process
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 365
ChainResidue
AASP16
AHIS204
AHIS206
AASN240
AHOH369
AHOH497

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 366
ChainResidue
AHOH492
AHOH493
AHOH494
AHOH495
AALA191
AILE278
AHOH491

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 367
ChainResidue
AARG15
AGLU143
AHOH450
AHOH469
AHOH471
AHOH496
AHOH532

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 368
ChainResidue
APRO94
ALYS95
ALYS96
ATHR135
AASP136
AHOH537

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 365
ChainResidue
BASP16
BHIS204
BHIS206
BASN240
BHOH370
BHOH421

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 366
ChainResidue
BALA24
BHOH479
BHOH480
BHOH481
BHOH482
BHOH483

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 367
ChainResidue
BARG15
BSER141
BGLU143
BHOH457
BHOH491
BHOH511

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 368
ChainResidue
BARG6
BGLY41
BASP43
BLYS69
BGLY262
BHOH447

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 369
ChainResidue
BPRO94
BLYS95
BLYS96
BTHR135
BASP136
BHOH463

Functional Information from PROSITE/UniProt
site_idPS00815
Number of Residues17
DetailsAIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGeQspgaAmtkeeK
ChainResidueDetails
ALEU14-LYS30

site_idPS00816
Number of Residues14
DetailsAIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. WsaHcHNDlGlAvA
ChainResidueDetails
ATRP201-ALA214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000269|PubMed:22352945, ECO:0007744|PDB:3RMJ
ChainResidueDetails
AASP16
AHIS204
AHIS206
AASN240
BASP16
BHIS204
BHIS206
BASN240

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon