Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RJL

Crystal structure of 1-pyrroline-5-carboxylate dehydrogenase from Bacillus licheniformis (Target NYSGRC-000337)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
A	0004657	molecular_function	proline dehydrogenase activity
A	0006537	biological_process	obsolete glutamate biosynthetic process
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
B	0004657	molecular_function	proline dehydrogenase activity
B	0006537	biological_process	obsolete glutamate biosynthetic process
B	0009898	cellular_component	cytoplasmic side of plasma membrane
B	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
C	0004657	molecular_function	proline dehydrogenase activity
C	0006537	biological_process	obsolete glutamate biosynthetic process
C	0009898	cellular_component	cytoplasmic side of plasma membrane
C	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
D	0004657	molecular_function	proline dehydrogenase activity
D	0006537	biological_process	obsolete glutamate biosynthetic process
D	0009898	cellular_component	cytoplasmic side of plasma membrane
D	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
E	0004657	molecular_function	proline dehydrogenase activity
E	0006537	biological_process	obsolete glutamate biosynthetic process
E	0009898	cellular_component	cytoplasmic side of plasma membrane
E	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
E	0016491	molecular_function	oxidoreductase activity
E	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
F	0004657	molecular_function	proline dehydrogenase activity
F	0006537	biological_process	obsolete glutamate biosynthetic process
F	0009898	cellular_component	cytoplasmic side of plasma membrane
F	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
F	0016491	molecular_function	oxidoreductase activity
F	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
G	0004657	molecular_function	proline dehydrogenase activity
G	0006537	biological_process	obsolete glutamate biosynthetic process
G	0009898	cellular_component	cytoplasmic side of plasma membrane
G	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
G	0016491	molecular_function	oxidoreductase activity
G	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
H	0004657	molecular_function	proline dehydrogenase activity
H	0006537	biological_process	obsolete glutamate biosynthetic process
H	0009898	cellular_component	cytoplasmic side of plasma membrane
H	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
H	0016491	molecular_function	oxidoreductase activity
H	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 539

Chain	Residue
A	GLU343
A	HOH557
A	HOH587
B	GLU343

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD A 540

Chain	Residue
A	ASP393

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 541

Chain	Residue
A	GLU352
A	HOH803
B	GLU16
B	HOH802

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 542

Chain	Residue
A	SER429
A	GLU433

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CD A 543

Chain	Residue
A	ASP432
A	HOH634
A	HOH635
A	HOH636
D	ASP455
D	CD539
D	ACT544
D	HOH797

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 544

Chain	Residue
A	ASP455
D	GLU436

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD A 545

Chain	Residue
A	GLU224
A	ACT548
D	LYS108

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 546

Chain	Residue
A	ASP94
A	GLU96

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 547

Chain	Residue
A	GLU298
D	ASP299
D	ASN453
D	HIS456

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 548

Chain	Residue
A	LYS108
A	ARG111
A	GLU224
A	CD545
D	GLU224
D	HOH799

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD B 539

Chain	Residue
B	LYS108
B	GLU224
B	ACT543
B	HOH638
B	HOH639
B	HOH801

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 540

Chain	Residue
B	GLU352
B	HOH662
B	HOH663
B	HOH664

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 541

Chain	Residue
B	ASP297
B	GLU298
B	HIS456
C	GLU298

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 542

Chain	Residue
B	GLU400
B	HOH659
B	HOH660
B	HOH661

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 543

Chain	Residue
B	LYS108
B	GLU224
B	CD539
B	HOH801

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD C 539

Chain	Residue
B	LYS108
B	HOH800
C	GLU224
C	HOH678

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD C 540

Chain	Residue
C	GLU343

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD C 541

Chain	Residue
C	GLU433

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD C 542

Chain	Residue
C	GLU23
C	HOH677
C	HOH812
D	GLU16
D	CD543

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD C 543

Chain	Residue
C	ASP74
G	ASP74

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD C 544

Chain	Residue
C	ASP94
C	GLU96

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD C 545

Chain	Residue
C	GLU162
C	HOH825
C	HOH826

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD C 546

Chain	Residue
C	ASP374
C	HOH827
C	HOH828
C	HOH829

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD C 547

Chain	Residue
C	ASP432
C	CD549
C	HOH813
C	HOH814
C	HOH816
C	HOH830

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD C 548

Chain	Residue
B	GLU436
C	ASP455

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD C 549

Chain	Residue
B	ASP432
C	HIS456
C	CD547
C	HOH816
C	HOH817
C	HOH818

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD D 539

Chain	Residue
A	HIS456
A	CD543
D	ASP432
D	ACT544
D	HOH797

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD D 540

Chain	Residue
D	GLU224
D	HOH716
D	HOH718
D	HOH798
D	HOH799

site_id	DC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD D 541

Chain	Residue
A	ASP432
D	ASP455

site_id	DC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 542

Chain	Residue
A	HOH550
D	ASP94
D	GLU96
D	HOH571

site_id	DC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD D 543

Chain	Residue
C	GLU16
C	CD542
D	ARG19

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT D 544

Chain	Residue
A	ARG459
A	CD543
A	HOH635
D	ARG459
D	CD539

site_id	DC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD E 539

Chain	Residue
E	ASP432
E	ACT544
E	ACT545
E	HOH791
G	HIS456
G	HOH809

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD E 540

Chain	Residue
E	GLU352
E	HOH794
F	GLU16
F	HOH795

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD E 541

Chain	Residue
E	GLU343
E	HOH555
F	GLU343
F	HOH583

site_id	DC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD E 542

Chain	Residue
E	GLU224
E	HOH819
E	HOH820
E	HOH821

site_id	EC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD E 543

Chain	Residue
E	GLU436
G	ASP455

site_id	EC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT E 544

Chain	Residue
E	ASP432
E	HIS456
E	CD539
E	HOH791
G	GLU298
G	ASN453
G	HIS456
G	HOH808

site_id	EC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT E 545

Chain	Residue
E	ASP432
E	CD539
G	ASP455
G	HIS456
G	ARG459
G	HOH807
G	HOH809

site_id	EC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD F 539

Chain	Residue
F	ACT543
F	ACT544
F	HOH824
H	CD539
H	ACT542

site_id	EC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD F 540

Chain	Residue
F	GLU224
H	LYS108

site_id	EC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD F 541

Chain	Residue
F	ASP393

site_id	EC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD F 542

Chain	Residue
F	ASP455

site_id	EC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT F 543

Chain	Residue
F	GLU298
F	HIS456
F	CD539
F	HOH824
H	HIS456
H	CD539

site_id	EC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT F 544

Chain	Residue
F	ASP432
F	ARG459
F	CD539
F	HOH824
H	ASP455
H	ACT542

site_id	FC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD G 539

Chain	Residue
G	GLU433

site_id	FC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD G 540

Chain	Residue
E	ASP299
E	HIS456
E	HOH550
G	GLU298
G	HOH806

site_id	FC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD G 541

Chain	Residue
G	ASP432
G	HOH807
G	HOH808
G	HOH809

site_id	FC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD G 542

Chain	Residue
G	GLU16
G	CD543
H	HOH823

site_id	FC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD G 543

Chain	Residue
G	GLU23
G	CD542
G	HOH822
H	GLU16
H	HOH823

site_id	FC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD G 544

Chain	Residue
G	ASP94
G	GLU96

site_id	FC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD H 539

Chain	Residue
F	HIS456
F	CD539
F	ACT543
H	ASP432
H	ACT542

site_id	FC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD H 540

Chain	Residue
H	GLU224
H	HOH597

site_id	FC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD H 541

Chain	Residue
H	ASP94
H	GLU96
H	HOH547

site_id	GC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT H 542

Chain	Residue
F	HIS456
F	ARG459
F	CD539
F	ACT544
H	ARG459
H	CD539

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgFAGQKCSAGS

Chain	Residue	Details
A	PHE314-SER325

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. AEMGGKDT

Chain	Residue	Details
A	ALA286-THR293

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00733","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)